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Collagen: A review on its sources and potential cosmetic applications
Journal of Cosmetic Dermatology
Abstract
Collagen is a fibrillar protein that conforms the conjunctive and connective tissues in the human body, essentially skin, joints, and bones. This molecule is one of the most abundant in many of the living organisms due to its connective role in biological structures. Due to its abundance, strength and its directly proportional relation with skin aging, collagen has gained great interest in the cosmetic industry. It has been established that the collagen fibers are damaged with the pass of time, losing thickness and strength which has been strongly related with skin aging phenomena [Colágeno para todo. 60 y más. 2016. http://www.revista60ymas.es/InterPresent1/groups/revistas/documents/binario/ses330informe.pdf.]. As a solution, the cosmetic industry incorporated collagen as an ingredient of different treatments to enhance the user youth and well-being, and some common presentations are creams, nutritional supplement for bone and cartilage regeneration, vascular and cardiac reconstruction, skin replacement, and augmentation of soft skin among others [J App Pharm Sci. 2015;5:123-127]. Nowadays, the biomolecule can be obtained by extraction from natural sources such as plants and animals or by recombinant protein production systems including yeast, bacteria, mammalian cells, insects or plants, or artificial fibrils that mimic collagen characteristics like the artificial polymer commercially named as KOD. Because of its increased use, its market size is valued over USD 6.63 billion by 2025 [Collagen Market By Source (Bovine, Porcine, Poultry, Marine), Product (Gelatin, Hydrolyzed Collagen), Application (Food & Beverages, Healthcare, Cosmetics), By Region, And Segment Forecasts, 2014 – 2025. Grand View Research. http://www.grandviewresearch.com/industry-analysis/collagen-market. Published 2017.]. Nevertheless, there has been little effort on identifying which collagen types are the most suitable for cosmetic purposes, for which the present review will try to enlighten in a general scope this unattended matter.
... Except that, the major challenge remains to choose between biomaterials from animal and/or non-animal sources. Chitosan, collagen and silk are the main animalsourced biomaterials widely discussed in the literature (Avila Rodríguez et al., 2018;Qi et al., 2017;Tian et al., 2022). Thanks to their qualities, these materials can adopt various forms such as films, hydrogels and sponges to respond to the needs of specific applications. ...
... Collagen is represented as the most abundant structural protein in the human body, accounting for around 25% to 35% of protein mass. Indeed it has been shown that any protein characterized by a structure based on three helical polypeptide chains ( Figure 1) belong to the collagen family (Avila Rodríguez et al., 2018). Collagen is a viscoelastic material with high tensile strength and low extensibility. ...
... Collagen sources include chicken skin, bone, duck feet, equine tendons, bird feet, sheep skin, frog skin, and many others (Aleksandra et al., 2020). However, collagen from some sources is misfolded, which can lead to disease (Avila Rodríguez et al., 2018). Its availability in nature makes it of even greater interest, as it is used in various fields including biomedical, particularly in blood coagulation, tissue remodeling and vascular prostheses, generally in the form of microparticles that are easy to inject subcutaneously, or as tissue scaffolding (François Portier, 2017). ...
The application of biomaterials in the biomedical field represents a major advancement, offering effective and sustainable alternative solutions. These materials stand out for their unique properties, particularly their biocompatibility and biodegradability. However, the choice between animal or non-animal sources constitutes a primary challenge, directly influencing their use and effectiveness in various contexts. This chapter offers a comparative analysis of biomaterials of animal and non-animal origin, highlighting their distinct properties and adaptability to biomedical applications, while mentioning the limitations of each type of source. This multidimensional analysis thus provides a critical framework for guiding the choice of biomaterials based on the specific needs of biomedical applications and opens up perspectives on the development of hybrid or alternative materials capable of overcoming these limitations.
... В процессе коллагеногенеза выделяют несколько этапов: рибосомальный синтез полипептидной цепи препро-α-цепей коллагена, их гидроксилирование, гликозилирование, формирование проколлагена, поступление во внеклеточный матрикс протоколлагена с удалением Nи C-концевых доменов, формирование во внеклеточной среде микрофибрилл с предварительным окислительным дезаминированием некоторых радикалов лизина и, наконец, образование с участием гиалуроновой кислоты и протеогликанов сложных волокнистых структур-фибрилл, волокон и волокнистого каркаса ткани [28][29][30][31][32]. ...
... Молекулярный шаперон эндоплазматического ретикулума НSР47 действует на нескольких этапах созревания коллагена: предотвращает агрегацию и разложение вновь образованных цепей проколлагена, ускоряет образование трёхспиральной структуры и стабилизирует её, содействует секреции коллагена [8,18,20,22,26,27,29]. Введение экзогенного коллагена типа I крупного рогатого скота приводит к значительному увеличению денситометрических параметров, статистически значимому увеличению уровня экспресии белка НSР47 и гена Р4НА1, также отмечается перестройка цитоскелета в обработанных клетках с образованием чётко расположенных нитей актина и удлинением формы клеток [1,8,18,20,22,26,27,[29][30][31][32]. Стимуляция, способствующая усилению синтеза коллагена фибробластами, также приводит к усилению процессов деструкции вновь произведённого коллагена (преимущественно через стимуляцию MMP). ...
... Неишемические осложнения могут зависеть от техники введения и включать реакции в месте инъекции, нарушение контура, воспалительные и инфекционные процессы. В большинстве случаев данные негативные эффекты регрессируют в течение 2-7 дней [28, [30][31][32]. Следует также отметить, что результаты лечения зависят от грамотного подбора концентрации препаратов в зависимости от уровня снижения эластичности кожи, в том числе соблюдения техники разведения и введения препаратов [7,30,31]. ...
Aesthetic medicine is one of the most dynamically developing areas of modern healthcare. Today, injectable cosmetology provides an opportunity for a pathogenetic approach to correcting age-related skin changes and solving a number of aesthetic problems. Most often, preparations containing hyaluronic acid, micronized collagen, vitamins, amino acids, and trace elements are used for this purpose. This article presents an analysis of literature data devoted to the study of modern aspects of the use and effectiveness of injectable preparations based on hyaluronic acid modified with amino acids and preparations based on micronized collagen in aesthetic cosmetology. Keywords: modified hyaluronic acid, amino acids, micronized collagen, neocollagenogenesis, age-related changes in facial skin, fillers.
... Waste materials are minimized by recovering them to create high-value-added products [6,7]. Unfortunately, despite their availability and low cost, some sources can cause allergies or diseases such as osteogenesis imperfecta [3]. Without the risk of zoonoses such as spongiform encephalopathy (BSE) or foot-and-mouth disease (FMD), marine collagen appears to be safer [8]. ...
... However, recombinant technologies are associated with high costs, low yields, and cofactors crucial for the stable formation of biofunctional and bioactive collagens. This fact again argues in favor of the application of animal collagen in research and clinical settings [3]. ...
... The ever-increasing global demand for collagen in the dental surgery, tissue engineering, bone grafting, pharmaceuticals, food, and cosmetic industries has been estimated at USD 6.63 billion by 2025, while the global market for marine collagen, for example, is expected to have an annual growth rate of 7.39% by 2026 [2]. The source of collagen can be categorized into natural sources of animal or plant origin or through recombinant protein production systems, including yeasts, bacteria, mammalian cells, insects, plants, and even artificial fibrils that mimic the properties of collagen [3]. The predominant source of collagen is from animal sources, such as cattle, pigs, chickens, marine, or freshwater organisms, and hyaluronic acid, which leads to the formation of wrinkles [14]. ...
The circular economy of animal by-products rich in collagen focuses on converting collagen into peptides with a defined molecular weight. Collagen hydrolysates prepared by biotechnological methods from chicken gizzards, deer tendons, and Cyprinus carpio skeletons can be an alternative source of collagen for cosmetic products that traditionally use bovine or porcine collagen hydrolysates. Collagen hydrolysates were characterized by antioxidant activity, surface tension, solution contact angle, and other parameters (dry weight, ash content, and solution clarity). Furthermore, the vibrational characterization of functional groups and their molecular weight was performed using the GPC-RID method. Subsequently, emulsion and gel cosmetic matrices were prepared with 0.5% and 1.5% collagen hydrolysates. Microbiological stability, organoleptic properties, and viscosity were investigated. Verification of the biophysical parameters of the topical formulations was performed in vivo on a group of volunteers by measuring skin hydration and pH and determining trans-epidermal water loss. Fish collagen hydrolysate was the most suitable for cosmetic applications in the parameters investigated. Moreover, it also effectively reduces wrinkles in the periorbital region when used in a gel matrix.
... This makes HC highly digestible and easily absorbed. Moreover, in the dermis, HC supplies amino acids for collagen and elastin formation and stimulates fibroblasts to produce new collagen, elastin, and hyaluronic acid, making it ideal for cosmetic applications (Sibilla et al. 2015;Avila Rodríguez et al. 2018). ...
... Collagen can be extracted from different sources, such as vertebrates and invertebrates. The most common terrestrial sources are cattle, pigs, poultry (Avila Rodríguez et al. 2018), and marine organisms (particularly fish scales (Fan et al. 2013) and fish skin; Karami et al. 2019;Akram and Zhang 2020;Yousefi et al. 2017;Silvipriya et al. 2015) (Fig. 5). ...
... For these reasons, collagen represents one of the most important ingredients for cosmetic formulations thanks to the moisturizing, regenerating, and film-forming properties. Its versatility and ability to be used in relatively low concentrations but with significant impacts on the finished products make it a valuable component (Avila Rodríguez et al. 2018). ...
This review provides a general overview of collagen structure, biosynthesis, and biological properties, with a particular focus on marine collagen sources, especially fisheries discards and by-catches. Additionally, well-documented applications of collagen are presented, with special emphasis not only on its final use but also on the processes enabling sustainable and safe recovery from materials that would otherwise go to waste. Particular attention is given to the extraction process, highlighting key aspects essential for the industrialization of fish sidestreams, such as hygiene standards, adherence to good manufacturing practices, and ensuring minimal environmental impact. In this context, the EcoeFISHent projects have provided valuable insights, aiming to create replicable, systemic, and sustainable territorial clusters based on a multi-circular economy and industrial symbiosis. The main goal of this project is to increase the monetary income of certain categories, such as fishery and aquaculture activities, through the valorization of underutilized biomass.
... It is widely available, biologically active, and has moderate extraction costs, making it a key ingredient in cosmetics and pharmaceuticals. [12][13][14] Docosahexaenoic acid (DHA), derived from fish, is essential for brain and eye health, with high availability and moderate extraction challenges, making it a popular addition to cognitive and visual health supplements. Astaxanthin, a powerful antioxidant from microalgae and krill, is used for its anti-inflammatory and UV-protective effects, particularly in skin care products. ...
... Furthermore, marine lipids can serve as carriers for targeted drug delivery by leveraging their affinity for specific tissues or receptors (Table 4). 10,14,15 In addition to natural marine-derived biomaterials, researchers have explored their modification to enhance drug delivery capabilities. Chemical cross-linking techniques have been Figure 1. ...
Marine environments offer a rich and diverse array of resources, including unique biomaterials with exceptional properties applicable in biomedicine. This review explores marine-derived functional biomaterials and their significance in biomedicine and drug delivery. Marine organisms have evolved unique characteristics to adapt to their environment, resulting in the production of bioactive compounds and biomaterials distinguished by their characteristics such as biocompatibility, bioactivity, and regenerative potential. These biomaterials encompass various compounds, such as proteins, polysaccharides, lipids, and minerals, obtainable from diverse marine sources like algae, crustaceans, mollusks, and deep-sea organisms. This review covers the extraction, processing, and modification techniques used to harness these functional biomaterials. Additionally, it highlights their versatile applications in biomedicine, including tissue engineering, drug delivery, wound healing, and implantable medical devices. The unique physicochemical properties of marine-derived biomaterials provide advantages over terrestrial counterparts, rendering them particularly promising for innovative biomedical applications. Despite the considerable potential of marine-derived biomaterials, certain challenges require attention, such as sustainable sourcing, standardization of extraction methods, and regulatory considerations. Collaborative efforts among biologists, materials scientists, and biomedical researchers are essential for fully realizing the potential of these biomaterials in advancing medical technology. Leveraging these inherent properties can lead to groundbreaking advancements in regenerative medicine and the development of more effective and sustainable biomedical devices and therapies.
... Collagen (I to XXVIII) is a structural protein present throughout the human body, conformed by three polypeptide fibrils that form a triple helix structure, with a diameter of 10-500 nm each and a molecular weight around 285 kDa [40]. Even though there are 28 collagen types identified today, the most abundant in the human body are collagen I, II, and III [40,83,84]. ...
... Collagen (I to XXVIII) is a structural protein present throughout the human body, conformed by three polypeptide fibrils that form a triple helix structure, with a diameter of 10-500 nm each and a molecular weight around 285 kDa [40]. Even though there are 28 collagen types identified today, the most abundant in the human body are collagen I, II, and III [40,83,84]. ...
For organ-on-a-chip (OoC) engineering, the use of biocompatible coatings and materials is not only recommended but essential. Extracellular matrix (ECM) components are commonly used as coatings due to their effects on cell orientation, protein expression, differentiation, and adhesion. Among the most frequently used coatings are collagen, fibronectin, and Matrigel, according to the specific cell type and intended OoC application. Additionally, materials such as polydimethylsiloxane (PDMS), thermoplastics, chitosan, and alginate serve as scaffolding components due to their biomechanical properties and biocompatibility. Here, we discuss some of the most employed coating techniques, including SAMs, dip coating, spin coating, microcontact printing, and 3D bioprinting, each offering advantages and drawbacks. Current challenges comprise enhancing biocompatibility, exploring novel materials, and improving scalability and reproducibility.
... Collagen, a pivotal protein of the extracellular matrix in many tissues and organs, accounts for about 30% of total protein in the human body, with the most abundant types I, II, and III being present in knee meniscus, auricular cartilage, and intervertebral disk (Bielajew, Hu, and Athanasiou 2020). The various types and functions of collagens have been well documented (Avila Rodriguez, Barroso, and Sanchez 2018). For example, the fibrilforming collagen can be divided into types I, II, III, V, and XI, with the type II collagen mainly distributed in cartilage, cornea, lung, vessel wall, nucleus, and reticular fibers, type I collagen in bone, tendon, cornea and ligaments, and type III collagen in bone, skin, vitreous body, and pulposus (Avila Rodriguez, Barroso, and Sanchez 2018). ...
... The various types and functions of collagens have been well documented (Avila Rodriguez, Barroso, and Sanchez 2018). For example, the fibrilforming collagen can be divided into types I, II, III, V, and XI, with the type II collagen mainly distributed in cartilage, cornea, lung, vessel wall, nucleus, and reticular fibers, type I collagen in bone, tendon, cornea and ligaments, and type III collagen in bone, skin, vitreous body, and pulposus (Avila Rodriguez, Barroso, and Sanchez 2018). Moreover, the main functions of type II collagen are for cartilage repair and arthritis treatment, while those of type I collagen are for guided tissue regeneration and type III collagen for hemostats and tissue sealants (Avila Rodriguez, Barroso, and Sanchez 2018). ...
This study aims to extract pepsin soluble collagen (PSC) from sturgeon cartilage, hydrolyze to sturgeon cartilage collagen peptides (SCCP), and prepare SCCP nanoliposomes to explore the treatment effects of osteoarthritis (OA) in rats. PSC was extracted using 0.5 M acetic acid and pepsin (10%) and enzymatically hydrolyzed with 4.5% alcalase plus 4.5% flavourzyme to obtain SCCP. Amino acid analysis revealed the presence of glycine, proline, and hydroxyproline in high amounts, while SDS‐PAGE showed that the PSC belonged to type II collagen with molecular weight (MW) of SCCP being <2 kDa and MALDI‐TOF‐MS indicated the MW distribution to range from 302.594 to 683.050 Da with the peptide fragments <500 Da accounting for 89.71%. SCCP nanoliposomes composed of phosphatidylcholine, fatty acid sucrose ester, glycerol, and deionized water were prepared with size at 34.58 nm, polydispersity index at 0.19, zeta potential at ‐54.53 mV, and encapsulation efficiency at 88.14%. Tube feeding of SCCP/SCCP nanoliposomes into OA rats alleviated pain responses by joint damage through reduction in hind limb weight‐bearing difference, knee joint width difference, and levels of serum biomarkers including CTX‐II, TGF‐β1, PIICP, and COMP. Histopathologic images demonstrated the mitigation of joint damage symptoms in the tissue by reducing cartilage joint damage, inhibiting chondrocyte apoptosis, promoting chondrocyte regeneration, and reducing synovitis. Collectively, the high dose of SCCP nanoliposomes was the most effective in alleviating OA possessing a great potential to be developed into a health food or botanic drug for the treatment of joint‐related disease.
... MMP1 can almost completely degrade type I and III collagen, and MMP9 further degrades the collagen fiber fragments produced by MMP-1 [57]. MMP3 degrades type IV collagen, proteoglycans, and fibronectin [57]. ...
... MMP1 can almost completely degrade type I and III collagen, and MMP9 further degrades the collagen fiber fragments produced by MMP-1 [57]. MMP3 degrades type IV collagen, proteoglycans, and fibronectin [57]. ...
Ultraviolet (UV) irradiation causes skin wrinkles and decreases elasticity. UV also increases binding between advanced glycation end products (AGEs) and the receptor for AGEs (RAGE), resulting in increased inflammation and activation of NF-κB. We evaluated whether fermented fish collagen (FC) could decrease photoaging via decreasing AGE–RAGE binding activity, which was associated with decreased TNF-α and NF-κB levels in UV-irradiated keratinocytes and animal skin. In the UV-irradiated keratinocytes, AGE–RAGE binding activity and TNF-α secretion levels were increased, and FC decreased these. Additionally, AGE–RAGE binding activity and TNF-α secretion levels were attenuated by soluble RAGE (RAGE inhibitor) in the UV-irradiated keratinocytes. FC decreased AGE–RAGE binding activity, TNF-α levels, and translocation of NF-κB in the UV-irradiated skin. Furthermore, FC decreased the expression of matrix metalloproteinases 1/3/9, which degrades collagen fibers, and Smad7, which inhibits Smad2/3, in UV-irradiated skin. FC increased Smad2/3 and collagen fiber accumulation. FC also increases skin moisture and elasticity. In conclusion, FC could attenuate skin photoaging via decreasing AGE–RAGE binding activity and its downstream signals such as TNF-α and NF-κB.
... The lack of collagen as part of human organisms and tissues contributes to one of the main causes leading to the aging of tissues, the deterioration of organ function, and the onset of chronic illnesses [1]. The supplementation of collagen is a significant method for minimizing the effects of aging while encouraging optimal wellness [2][3][4]. ...
Fish gelatin (FG) is a promising alternative to mammalian gelatin but is limited by poor gelling ability, low gel strength, and inability to set at room temperature. This study evaluated the effects of furcellaran (FUR), a gelling agent, on the structural and physicochemical properties of FG gels at different substitution levels (25–100%). The addition of 25% FUR improved gel strength and hardness. However, higher FUR levels (>50%) led to reduced springiness and increased syneresis. Intermolecular force measurements revealed that ionic and hydrogen bonds were crucial in the FG/FUR gel system, with higher levels of FUR promoting stronger ionic and hydrogen bonding. Color changes were observed with decreased L* and increased b* and ∆E* values as FUR levels rose. Gelling and melting points also increased proportionally with FUR content. Microstructural analysis showed denser gel networks with smaller gaps upon FUR incorporation. SAXS analysis confirmed enhanced structural conformation with higher FUR levels. An appropriate level of FUR added (25%) could therefore improve gelling properties via increasing gel strength and gelling temperature without negative effects on springiness and syneresis of resulting gel.
... For the past five decades, collagen-based materials have proven valuable across multiple industries (Shekhter et al., 2019). Collagen derivatives, prominent in the wellness industry, are recognized for their high biocompatibility and bioavailability, supplements, cosmetics, and therapeutic products (Avila Rodríguez et al., 2018). While CBJ has been identified as a good source of marine collagen, producing high-quality jellyfish collagen products with functional properties remains challenging due to the limited understanding of how processing conditions affect the final product's characteristics (Chiarelli et al., 2021;El Blidi et al., 2021). ...
... Contemporary aesthetic medicine predominantly utilises xenogeneic collagen sourced from animal derivatives, as exemplified by FDA-approved Zyderm ® -a standardised bovine-derived injectable filler containing 95% type I and 5% type III collagen fractions. This cross-species biomaterial is specifically engineered for deep dermal implantation targeting rhytid correction and volumetric restoration of facial contour depressions, demonstrating a therapeutic window of 3-6 months post-administration [12,13]. Current biomedical practice reveals that more than 98% of collagen employed in therapeutic formulations and tissue-engineered medical devices originates from animal sources, with bovine-derived variants maintaining priority in clinical applications due to established quality-controlled production pipelines and superior batch-to-batch reproducibility [14,15]. ...
This study introduces a novel recombinant humanised collagen (DuCol) developed through codon optimisation and prokaryotic soluble expression, exhibiting exceptional biocompatibility and bioactivity. Structural integrity was confirmed via RP-HPLC, SEM, and CD spectroscopy. In vitro evaluations revealed DuCol’s dose-dependent enhancement of NIH-3T3 fibroblast proliferation, adhesion, and migration. In a D-galactose-induced ageing rat model, subcutaneous implantation of DuCol showcased time-dependent anti-ageing effects. Early-stage intervention (30 days post-injection) markedly upregulated COL1A1 expression through the TGF-β/Smad3 pathway activation, outperforming poly-l-lactic acid (PLLA) in collagen deposition. Histological analysis revealed 23.4% greater dermal thickness in DuCol-treated groups compared to PLLA at 90 days. While PLLA exhibited sustained collagen stimulation beyond 90 days, DuCol exhibited superior early-phase efficacy (p < 0.001) with comparable safety profiles (no inflammatory response observed through 180-day monitoring). The combinatorial PLLA/DuCol (P&C) formulation synergistically enhanced dermal regeneration, achieving a 31.7% thicker collagen matrix than monotherapy groups. These results underscore the potential of DuCol as a novel implantable filler material for skin repair and regeneration.
... There are at least 28 distinct varieties of collagen known to exist [60]. About 90% of the dermis contains collagen types I and III, which are crucial for preventing skin aging [61]. According to Raab, Yatskayer, Lynch, Manco, and Oresajo (2017), collagen is the main structural component of skin extracellular matrix (ECM) and serves a functional purpose [62]. ...
Cosmetic business is one of the major billers of the global economy since it serves a market which is growing up continuously due to different reasons such as consumer behavior changes, technological and scientific developments, in addition to the rise in consumer awareness. This review focuses on giving an idea about the importance of the cosmetics industry some details about how the change in the customer demands encourages innovation in this sector. Nowadays, the growing awareness of the clean beauty is considered a trend, where the chemical-free, ethical, and sustainable products are of higher interest for most customers. It is worth to mention that the industrial practices for cosmetics are changing due to the developing personalized skincare and haircare products, as well as, environmentally friendly packaging, and the use of artificial intelligence in product creation and promotion. This review focuses on the use of nanotechnology in cosmetics and dermatology products. The use of nanotechnology helped in improving the active components' stability, penetration, and effectiveness. Particularly useful for sun protection anti-aging treatments, in addition to the targeted administration of active ingredients such as Nano emulsions, liposomes, and nanoparticles. This review offers a detailed information about the recent developments and trends in the cosmetics industry, focusing on how nanotechnology could be used to meet the changes in consumer needs taking into consideration sustainability and safety issues.
... Collagen's biocompatibility, biodegradability, and low immunogenicity make it widely used in wound repair, tissue engineering, and regenerative medicine (Du et al., 2021). However, natural collagen's clinical use is limited by viral transmission, immunogenicity, low extraction efficiency, poor solubility, and gelation issues (Avila Rodríguez et al., 2018;Yang et al., 2015). Recombinant collagen, designed based on the amino acid sequence of natural collagen, has been developed using synthetic biology techniques, allowing for the production of collagen within engineered cells. ...
Objective
This study aimed to chemically synthesize a homotrimeric collagen peptide, evaluate its safety, and assess its effectiveness in promoting collagen synthesis.
Methods
A homotrimeric collagen peptide was synthesized and structurally characterized using circular dichroism and infrared spectroscopy. Thermal stability was analyzed by TG-DSC, and molecular weight and amino acid composition were determined. In vitro cytotoxicity testing assessed safety, while UV-induced photoaging experiments evaluated its effects on collagen and elastin synthesis. In vivo studies in BALB/c mice examined its impact on collagen content, skin structure, and angiogenesis.
Results
The synthesized collagen peptide exhibited high purity (99.1%) and an amino acid composition of glycine, proline, and hydroxyproline in a balanced ratio (15:17:13). Structural analysis confirmed a stable triple-helical conformation similar to type I collagen with excellent thermal stability (Tm = 326.15°C). Cytotoxicity testing showed no adverse effects on cell viability. In vitro, the peptide significantly enhanced collagen and elastin synthesis in fibroblasts. In vivo, intradermal and subcutaneous injection increased collagen content, improved skin structure, and enhanced microvessel density.
Conclusion
This study presents a chemically synthesized homotrimeric collagen peptide with superior purity, structural stability, and biological efficacy in promoting collagen synthesis. Compared to previous studies, this biomimetic material exhibits exceptional thermal stability (Tm = 326.15°C) and a well-balanced amino acid composition, enabling applications in cosmetics and medical devices requiring heat sterilization (e.g., autoclaving), as validated by our patented method (China Patent No. ZL202410309842.9).
... Among them, collagen type I constitutes approximately 85% of total collagens [19]. Collagen type I is most commonly used in product manufacturing in a variety of cosmetic applications due to its high biocompatibility [20], making it an excellent target in the antiaging process. Therefore, this study evaluates how much type I collagens were synthesized. ...
Aging is one of the inevitable problems people face, age can cause significant change in skin, both inside and out. As such, ingredients that can delay the aging of skin are highly valued. There are many peptides that have been found to be beneficial to human health, they can reduce the risk of diseases and can be used as anti-aging ingredients. Previous studies have evaluated collagen tripeptide and chicken protein hydrolysate. The studies reported that collagen tripeptide and chicken protein hydrolysate can enhance wound healing and improve physical stamina, respectively. Collagen tripeptide and chicken protein hydrolysate have the potential for applications in a variety of fields. In this study, reconstructed human epidermal were used in vitro skin irritation tests to test anti-aging and whitening effects, and the tests were used to evaluate the safety and efficacy of collagen tripeptide and chicken protein hydrolysate. The results showed that collagen tripeptide and chicken protein hydrolysate were non-irritant. At 20 mg/mL, the collagen type I synthesis of chicken protein hydrolysate and collagen tripeptide were increased to 99.3% and 129.4% and promoted fibroblast proliferation to 62.2% and 22.1%. 4 mg/mL of chicken protein hydrolysate can inhibit melanin production at 29.7% (with α-MSH stimulation). There is the potential for use in cosmetics, and may be a potential candidate for development in anti-aging and whitening.
... Over the past decades, a variety of natural compounds from animal origins have been systematically extracted, identified, and harnessed as dietary or therapeutic agents to treat, prevent, and alleviate a spectrum of diseases and health conditions . Among the proteins and peptides derived from animals, collagen from fish, bovine, and porcine skin is notable for its effects on skin and joint health and is widely used in cosmetics and dietary supplements (Avila Rodríguez et al., 2018). Gelatin, obtained from animal bones, skins, and connective tissues, serves as a food-gelling agent and aids in wound healing, with applications in the food industry and pharmaceutical formulations (Alipal et al., 2021). ...
Bioactive compounds are naturally occurring chemicals that exert significant biological effects, including therapeutic and preventive actions against diseases. These compounds play a crucial role in synthesizing essential biomolecules and modulating biological functions, making them invaluable in various fields of health and science. This chapter systematically categorizes bioactive compounds based on their sources, which include plants, agro-industrial by-products, animals, and microbes. Each source contributes unique chemical properties and health benefits, making bioactive compounds highly versatile. Emphasis is placed on the biotechnological production of these compounds, utilizing advanced techniques such as microbial fermentation, plant cell culture, metabolic engineering, and recombinant DNA technology. These methodologies increase the efficiency of bioactive compound production and promote sustainability by reducing the need for natural harvesting, thus supporting biodiversity conservation efforts. The application section delves into the vast uses of bioactive compounds, particularly their role in developing innovative solutions across multiple industries such as pharmaceuticals, the food industry, cosmetics, and environmental management. In pharmaceuticals, bioactive compounds are pivotal in drug discovery and development of antibiotics, enzyme inhibitors, and vaccines, effectively demonstrating their capacity to treat and prevent a range of diseases. In the food industry, these compounds are critical for improving food safety and enhancing nutritional value by serving as natural alternatives to synthetic additives. Industrial applications highlight the role of bioactive compounds in producing biopolymers and biofuels, positioning them as key contributors to sustainable technological advancements. The chapter concludes by underscoring the importance of ongoing research into new sources of bioactive compounds and optimizing their properties for broader applications. Future directions propose enhancing biotechnological processes and expanding their utilization in environmental biotechnology to exploit further their potential in promoting human health and environmental sustainability. The chapter presents bioactive compounds as vital agents in bridging natural biological benefits with technological innovation, driving future advancements in science and industry.
... Collagen type III, which initially predominates in the wound area, udergoes gradual reorganizartion and is replaced by type I collagen, the mature form, within two to three weeks. As a result, on the seventh day, the amount of collagen III is elevated, whereas collagen type I increases by the twenty-first day [11]. The intracytoplasmic cytoskeleton of epithelial tissue typically contains the intermediate filament, a keratin-based element, known as cytokeratin (CK). ...
The prevalence of diabetic wound patients is increasing, rendering the management of these chronic wounds both costly and challenging. Zingerone a bioactive compound derived from ginger (Zingiber officinale) has antidiabetic and antioxidant properties. This study evaluated the therapeutic effects of Zingerone, alone and in combination with metformin, on diabetic wound healing in a rat model. The experimental groups: control wound (C), diabetic plus wound (D + W), plus Metformin (D + W + M), plus Zingerone (D + W + Z), and plus Metformin and Zingerone (D + W + M + Z). On the seventh, fourteenth, and twenty-first days of the study histological examinations (H&E, Masson Trichrome staining), immunohistochemistry for growth factors, collagen markers, and cytokeratin. biochemical analyses of oxidative stress, antioxidant enzyme levels and level of inflammation (ELISA) were conducted. In addition to lowering oxidative stress and inflammation, the results showed that the groups treated with Zingerone considerably improved tissue regeneration, angiogenesis, collagen formation, tissue maturation, and keratinization. Zingerone enhanced these therapeutic effects when used with metformin. These results demonstrate Zingerone’s promise as a therapeutic agent in the therapy of diabetic wounds and its capacity to improve healing results, especially when combined with metformin.
... Marine collagens have a characteristic triple helical structure like the mammalian collagens but with notable alterations in amino acid composition and thermal stability. These properties make marine collagens suitable for various biomedical, pharmaceutical, cosmetic, and food applications (Avila Rodríguez et al. 2018;Rastian et al. 2018). ...
Marine collagens have gained importance since collagen from mammalian sources has religious constraints and complications involving outbreaks of bovine spongiform encephalopathy and foot and mouth disease. Fish skin, bone, and scales have been the main sources of marine collagen. Recently, non-traditional sources such as starfish, jellyfish, sea urchins, and sea cucumbers have also been used to extract collagen. The conventional method for collagen extraction is tedious and demands considerable amounts of chemicals and extraction time. Sustainable collagen extraction with novel technologies has been looked upon, targeting more resource efficiency. The application of these novel technologies reduces the substantial quantities of chemicals used in collagen extraction in addition to reducing the extraction time without jeopardizing the collagen yield and functionality. In this chapter, we have dealt with information about non-traditional sources of collagen, especially aquatic ones, and broadly explained the novel technologies applied for the sustainable production of collagen from these sources and the effects of these technologies on collagen structure and functionality.
... The most prominent amino acids present in RFPs include glutamic acid, aspartic acid, alanine, lysine, glycine, γ-aminobutyric acid, and serine, all of which are essential for supporting skin hydration and barrier function [47,48]. In particular, certain amino acids, such as glycine, proline, and hydroxyproline, are critical components for collagen synthesis and play a vital role in maintaining skin health, elasticity, and structural integrity [49,50]. ...
With the growing demand for environmental sustainability, the cosmetics industry is increasingly turning to natural ingredients with high bioactivity and efficacy. Rice, a staple food in many cultures, particularly in Asia, is renowned for its nutritional and medicinal benefits, as well as its skincare properties. Numerous studies have emphasized the multifunctional benefits of rice in skincare, ranging from its ability to enhance hydration to its effectiveness in addressing signs of aging, positioning it as a promising ingredient in cosmetic formulations. Recently, fermentation has emerged as an innovative technique that significantly enhances the bioactive potential of rice. This process amplifies the production of beneficial compounds, such as organic acids, amino acids, polyphenols, polysaccharides, vitamins, and minerals. Previous studies have shown that rice fermentation products (RFPs) exhibit a range of skincare benefits, including moisturization, antioxidation, anti-inflammation, whitening, and anti-aging effects. This review provides an overview of the fermentation process and advantages of RFPs, followed by a detailed analysis of their key bioactive components and the diverse skincare benefits they offer. Moreover, we discuss the challenges related to the standardization, component analysis, and efficacy evaluation of these products, and we conclude with potential future research directions to fully explore the skincare potential of RFPs.
... Although collagen is found in many animal tissues, the most important source is cattle. Apart from this, it is obtained from sea creatures, plants, and also synthetic sources (Avila Rodríguez et al. 2018). Medical collagen, mostly type I, is currently derived from the dermis of several animals, including humans, pigs, sheep, horses, and bulls (Shekhter et al. 2019). ...
Throughout history, various human civilizations have used raw materials obtained from the body parts, metabolic byproducts, or non-animal components of animals as medical resources for the treatment of numerous diseases and relief of symptoms. Protein structures, including hormones and enzymes, as well as various animal-derived metabolites including polysaccharides, lipids, and vitamins, have been used for the development of raw drugs. These chemicals include widely used substances including heparin, melatonin, collagen, glucosamine, chondroitin, bile acids, and coenzyme Q10. Additionally, they include materials such as snake, spider, and amphibian poisons, which are now undergoing therapeutic development. This review presents examples of animal-derived pharmaceutical raw materials that are being used as drugs and have potential in drug development research. Detailed descriptions of the chemical structures, original sources and effects of these raw materials are included. In general, the production method that was previously carried out by using animal organisms has been replaced by the utilization of recombinant technologies. The use of animals as a resource in the drug development process is expected to remain an interesting topic and further research in this area is expected. Nevertheless, it is essential not to disregard the suggestions against utilizing animals in pharmaceutical production, particularly in cases where alternative sources are accessible.
... Type II is obtained from the tissue of vitreous body, cartilage, and nucleus pulposus, while Type III is derived from the vessel walls and reticular fibres of lungs, spleen, and liver and Type IV is derived from basement membranes. The tissues of marine invertebrates (Cnidaria and Porifera) contain are composed of about 60% of essential Type IV, V, and II collagen (Avila et al., 2018). Collagen fibres have a complex triple helix structure with stable inter-and intra-molecular hydrogen bond crosslinks (Sionkowska et al., 2017). ...
Marine resources offer a sustainable alternative to conventional protein and nutrient sources with marine collagen playing an important role in functional foods and nutritional supplements. Collagen from marine invertebrates is widely used in the food industry, pharmaceutical products, and biomedical applications. The aim of this study is to study the techniques used to extract collagen from various marine invertebrates. Marine collagen is a structural protein characterised by a helical structure composed of amino acids like glycine, proline, and hydroxyproline. Collagen comprises of 28 different types but only four types: Type I, II, III, and IV have always been studied. Type I is obtained from skin, tendon, and bone, meanwhile Type II is obtained from tissues of vitreous body, cartilage, and nucleus pulposus. Type III is obtained from the vessel walls and reticular fibres of lungs, spleen, and liver and Type IV is obtained from basement membranes. The extraction of marine collagen involves three stages: Pretreatment, extraction, and recovery. Several marine collagen extraction techniques are commonly used, including acid soluble collagen, pepsin soluble collagen, carbon dioxide acidified water, and alkaline denaturing procedures. Different extraction methods produce collagen yields with varying chemical compositions and characteristics. All of the extraction processes are ethical and environmentally friendly.
... Aging is a complex and multifactorial process accompanied by several functional and aesthetic changes on the skin, closely related to reducing elastin and collagen fibers, leading to fine lines and wrinkles [16][17][18][19]. The metabolism of collagen is ensured by a balanced process of synthesis, maturation, and degradation of collagen proteins that begins in the fibroblasts, continues in the extracellular matrix (ECM) and ends outside the cell, where ...
Background: Zanthoxylum piperitum (L.) DC., commonly known as Japanese pepper, is a deciduous shrub native to East Asia. Its berries are widely used as a spice, known for imparting a distinctive, tingly numbing sensation. Biologically, Z. piperitum has antimicrobial, antioxidant, and anti-inflammatory properties, and it is studied for its potential benefits in pain relief and digestive health. This study proposed a novel biotechnological Z. piperitum phytocomplex (ZPP) obtained by plant cell culture for skin health, specifically targeting collagen synthesis, extracellular matrix stability, and resilience against cellular stress. Given the bioactivity of Z. piperitum, we aimed to analyze its efficacy as a sustainable alternative for skin-supportive applications in cosmetics and supplements. Methods: ZPP was produced through stable plant cell cultures, yielding a lignan-rich (3.02% w/w) phytocomplex. Human fibroblasts (HFFs) were treated with varying ZPP concentrations to assess cellular viability, collagen metabolism, and ECM-related enzyme activities, both under normal and cell stress conditions. The in vivo assessment was performed by measuring biophysical skin parameters such as hydration, elasticity, and roughness in female volunteers for a period of six weeks. Results: In vitro, ZPP exhibited non-cytotoxicity at all concentrations tested. Under hyperosmotic stress, ZPP reduced cellular damage, suggesting enhanced resilience. ZPP upregulated lysyl oxidase (LOX) protein levels, critical for collagen cross-linking and ECM stability, with protective effects observed under oxidative/inflammatory conditions. Additionally, ZPP selectively inhibited collagenase, attenuating collagen breakdown, though antioxidant activity was modest. In vivo evaluation highlighted improved skin hydration, elasticity, and roughness. Conclusions: ZPP shows promise as a biotechnological agent for skin health, particularly in supporting collagen integrity, ECM stabilization, and cellular resilience under stress. While further studies are needed to explore its full efficacy, especially for aging and environmentally stressed skin, these findings highlight ZPP’s potential as a new ingredient for cosmetic formulations aimed at skin care and the treatment of alterations caused by aging or environmental conditions.
... Recombinant collagen is synthesised from mammalian, insect, and plant cells (Liu et al., 2021). Synthetic collagen has a similar structure to natural fibrils (Rodríguez, Barroso, Sánchez, 2018). ...
Collagen, the predominant protein in various organisms, is pivotal for tissue structure and mechanical properties. It has been extensively studied for its cosmetic, surgical, and anti-ageing applications, reflecting a growing interest in collagen-based cosmetics in Romania and prompting further research in this area. The study aimed to assess collagen’s efficacy and safety in dermocosmetology, comparing collagen peptides’ effectiveness in oral and topical applications. An analysis of the published studies on the subject was carried out, comparing the effectiveness of using collagen in different ways to improve skin conditions. The investigation included a literature review on collagen’s role in enhancing skin properties, covering its discovery, structure, chemical composition, systemic and topical applications, diverse sources, and skin penetration mechanisms. Hydrolysed collagen and its antioxidant properties are considered. The methods of investigating and monitoring the safety of cosmetic preparations are described. It has been concluded that topical collagen, similarly to nutraceutical supplements with collagen peptides, can slow down and reduce the signs of skin ageing and can increase skin elasticity, density, and moisture in equal measure. Studies have confirmed the harmlessness of collagen beyond doubt, but further investigation is necessary to determine the effectiveness of using different types of collagen.
... framework of a type of protein that or makes up the structure your Collagen is found in connective tissue, skin, tendons, bones, provides and cartilage. It structural support to tissues and plays an important role in cellular processes including tissue repair, immune response, cell communication, and cell migration, an essential process to maintain tissue [8]. Titanium dioxide (titania) (TiO2 synthetic a ) is It biomedical applications. ...
Polyvinyl alcohol (PVA) is a non-toxic, thermoplastic polymer that is completely biodegradable. So it is based on many composite materials for biomedical applications. In this study, various specimens were prepared by solvent casting method and then tested by tensile, FTIR, contact angle, SEM, antibacterial and cytotoxicity test. The results obtained showed the tensile strength decreased with the addition of PEG and then tended to improve after the addition of collagen and nano-titanium oxide. The wettability test shows the prepared specimens changed from hydrophobic to hydrophilic properties. The biological properties explained that the prepared composite had a better antibacterial effect and none of the samples had a toxic effect.
... The global market for collagen was approximately 3.71 billion USD in 2016 and is expected to double by 2025, particularly in the beverages, food, cosmetics, and healthcare sectors. Research has shown that collagen can be utilized in the production of biodegradable or edible films [106]. Seggiani et al., studied the potential use of hydrolyzed collagen in PBSA (butylene succinate-co-adipate)based blends, showing promise for creating compostable/ biodegradable films or molded products. ...
The growing global population, climate change and dietary patterns, and the demand for waste-free food production have increased the need for environmental protection. Packaging materials that have become more important to avoid food waste and environmental pollutants. Edible coatings and films used for preserving food are gaining popularity due to their eco-friendly nature and ability to carry active ingredients. Their use as antioxidant effectively help prevent quality deterioration by reducing oxidation and food spoilage. Edible packaging is now seen as a promising solution to extend shelf life of food products and reduce dependence on petroleum-based resources. Proteins are versatile materials suitable for producing edible and non-edible coatings and films. This article aims to provide a thorough overview of research on the use of proteins in food and edible packaging, including their modification, anti-oxidative, antimicrobial, and antifungal properties, as well as their economic implications.
Graphical Abstract
... Because there are no religious restrictions on their use and no reports of potentially transmissible diseases, marine organisms have recently drawn attention as promising sources of collagen. Specifically, the biomass obtained from fisheries and fishprocessing industries (fish and sea urchin wastes, undersized fish, and creatures that are caught by accident, such as sponges, jellyfish, sharks, and starfish) may prove to be a significant, albeit underutilized, collagen source 150,151,152,153,154,155 . The annual production of fish waste produced by the fish processing industries is estimated to be 25%. ...
The most prevalent protein in the human body, collagen is essential for preserving the structural soundness and functionality of different tissues. It is an essential part of connective tissues, which include skin, cartilage, bones, tendons, and ligaments. It also plays a key role in wound healing, cell signaling, and tissue repair. The many functions of collagen in human health and its connections to different illnesses are examined in this overview. It looks at the biochemical and structural characteristics of the many forms of collagen, the processes by which collagen is synthesized and broken down, and how imbalances can result in diseases including cardiovascular problems, fibrosis, osteoarthritis, and skin aging. There is also discussion of new treatment options, such as supplements, collagen-based biomaterials, and regenerative medicine techniques. New treatments targeted at promoting tissue repair, boosting quality of life, and avoiding collagen-related illnesses may be made possible by a better understanding of the many roles that collagen plays in both health and disease.
... Collagen and its supplements are natural sources of many nutrients important for life, such as amino acids, so taking them with thyroid medications may not cause a health problem. However, it should be noted that this is not always true (5). Many patients use collagen supplements to treat various diseases, including thyroid disorders Collagen supplements may interfere with thyroid medications and disrupt the body's physiology due to their potential to mimic the active hormone triiodothyronine (T3), a common medication in thyroid disorders (6). ...
The cosmetic industry is more concerned about the environmental, economic, and social impacts of the manufacturing and applications of cosmetic products. In the formulation of cosmetics, sustainability is addressed via sourcing and selection of the raw materials, which is achieved by replacing the synthetic chemical ingredients with sustainable natural alternatives. Therefore, herbal and natural cosmetics have gained huge recognition among the consumers who are more concerned about their health with beauty. A range of cosmetic products are available, and among them, skin cleanser is important as basic tool for self-care. Facial cleansers can be categorized into cream-based, gel-based, fluid-based, and powered-based. Skin-lightening and anti-aging agents like alpha-arbutin, ligninolytic enzymes (laccase, manganese peroxidase, lignin peroxidase), cytidine inhibitors, and all polyphenols extracted from natural resources are used in fairness creams, moisturizers, and sunscreens. Sunscreens are developed as inorganic blockers and organic absorbers to deal with skin premature aging due to UV radiations. All depigmentation agents like hydroquinine, kojic acid, and retinoic acid have wide applications in skin-lightening products. The natural active agents from different sustainable natural resources have been added in the cosmeceuticals to achieve the desired health benefits in accordance with sustainable development goals. Cosmetic formulations with natural active ingredients such as polyphenols, proteins, amino acids, natural colorant extracts, Gaur gur (GG)-based nanomaterial and nano-emulsion of arbutin loaded with coumaric acid have become widespread in cosmetic industry. Natural colorants gained attention in the cosmetic industry. These are extracted from plants leaves, flowers, roots, etc. In this chapter, we will discuss in detail the advancements in cosmetic science accordance with sustainable development goals via replacement of synthetic chemicals with natural, eco-friendly, and biodegradable alternatives.
Collagen synthesis is inextricably linked to skin health and is necessary for maintaining the skin's suppleness, structure, and general youthfulness. Wrinkles and loss of skin firmness are due to a reduction in collagen synthesis with age. The interest in dermatology lies in natural substances that promote collagen synthesis and prevent skin aging. Rich in bioactive compounds such as beta‐carotene, anthocyanins, and flavonoids, the root of sweet potato could be seen to offer the potential to enhance skin health. The review paper discusses the antioxidant and anti‐inflammatory properties of the root that protect the skin from oxidative stress and inflammation and delves into its use as a natural collagen formation and rejuvenation agent for the skin. Such in vitro and in vivo experiments and clinical studies provided experimental data on the effectiveness of this food supplement in skin health and collagen production. In addition, this review explored the role of natural sweet potato root, for instance, through the mechanism of sweet potato extract containing resveratrol in promoting skin health. This opens a chance for discussing the implications that supplements from the root of the sweet potato might make if orally administered and applied topically to improve health conditions for the skin.
ABSTRACT
Aim: The purpose of this research was to study the organization of collagen in animal skin in order to find similar SMAS structures.
Materials and Methods: The studies were conducted on skin samples from sheep and pigs (from the facial area), as well as trout. The obtained samples were studied under ultraviolet radiation. The Qscan Plus (AIOBIO, South Korea) device with a wavelength of 405 nm was used as a source of ultraviolet radiation. Skin sections were made at right and oblique angles in order to establish the spatial configuration of collagen fibers. The density (concentration) of fibers per unit area was calculated qualitatively by micro-and macroscopic methods with photometry. The results were evaluated in the Microsoft Office software package.
Results: In all the studied facial skin samples, the presence of collagen luminescent white in ultraviolet light was detected. The collagen was located laminarly, parallel to the skin surface, without the formation of a three-dimensional mesh structure characteristic of the SMAS of human facial skin. Conclusions: The data confirm the presence of collagen in the facial skin of the studied animals. However, unlike human facial skin, the characteristic three-dimensional collagen organization of the SMAS has not been detected. Further research is needed to determine the evolutionary origin of the SMAS and identify the factors that determine its formation.
Conclusion: No structures similar to SMAS were found in the animals used in the experiment. This is most likely due to the function performed by SMAS-the transmission of facial contractions to the skin. Probably, the structural organization of collagen on the human face is unique. Further research is required to accurately determine the evolutionary development of SMAS.
This study explores the innovative potential of recycled collagen derived from tannery waste for use in high-performance adhesive formulations. The leather industry generates significant amounts of solid waste, primarily from chromium-tanned leather, which poses substantial environmental challenges. Recent advancements in recycling techniques have opened new avenues for repurposing this waste, particularly through collagen extraction, which comprises about 30-35% of tannery residues. This research systematically reviews the methods and applications of collagen extraction, highlighting the material's versatility and environmental benefits when used as a bio-adhesive. The review identifies key challenges such as low water resistance, shear strength, and adhesiveness in collagen-based adhesives compared to synthetic counterparts. However, innovative solutions are emerging, including the incorporation of silane coupling agents and cross-linking technologies that significantly improve the water resistance and mechanical properties of these adhesives. Economic analyses further support the viability of using tannery waste-derived collagen in adhesive production, aligning with global sustainability goals and reducing reliance on petrochemical-based adhesives. Despite these advancements, the transition from laboratory research to commercial applications remains a significant challenge. Current Open Peer Review Approval Status Introduction The leather industry, particularly chromium-based tanning, generates substantial solid waste, including chromium sludge, chrome-tanned leather shavings, and trimmings, with only 20% of raw material converted into leather. 1-4 This results in significant waste, rich in collagen, which is often discarded in landfills due to the absence of cost-effective recycling programs. 5-7 Solid tannery waste, comprising around 25% untreated skin, contains approximately 30% to 35% collagen and 1.5% chromium, underscoring its potential for resource recovery. 8 India alone produces 0.02 million tons of chromium shavings annually (0.8 million tons of chromed leather trimmings per year), indicating a large potential resource for recycling into valuable products like renewed leather, 9 fertilizers in agriculture, composting,
Biologically active substances that come from animals and have positive impacts on human health are known as animal-based bioactives. The potential health advantages of bioactive compounds derived from animals have received considerable attention. These compounds include collagen, iron, conjugated linoleic acid, vitamin B12, omega-3 fatty acids, carnosine, creatine, etc. These bioactive substances exhibit potential health benefits such as immunomodulatory, anti-inflammatory, antibacterial, antioxidant, and anti-cancer properties. Advancements in this sector recently have illuminated the wide array of health advantages. Bioactive compounds derived from animals have increased scientific comprehension and created novel possibilities for their applications as functional foods, nutraceuticals, bioactive peptides to support gut health, and the development of drugs. To fully comprehend their modes of action, recommended dosages, and any side effects, more research is necessary. Developments in animal-based bioactives have demonstrated promise for use in nutrition, nutraceuticals, medicine, and functional foods. The objective of advancements and new trends is to develop innovative products from animal-based bioactive compounds that enhance overall health and wellness.
Marine food is on the rise due to an increase in capture and aquaculture worldwide. Marine food produces a large volume of waste because 50% of the food is not consumable; rather, it is traditionally disposed of in the environment. Therefore, different marine food species and waste have been studied to revitalize them and generate an economic impact. In this sense, diverse authors reported that marine food and waste are a rich source of bioactive compounds such as carotenoids, fatty acids, phenolic compounds, proteins, and vitamins, among other compounds. Therefore, different processes have been developed to extract these compounds, including conventional chemical extraction. However, a negative impact on the environment has been provoked, so alternative methods such as bioprocesses have been studied. Bioprocess as enzyme-assisted and fermentation are innovative processes that could be used as an alternative to conventional chemical extraction of bioactive compounds from marine food and waste because bioprocess methodologies with high purity and yield extraction have been developed.
Background
The reduction in collagen content within the subcutaneous fat layer due to aging results in thinning and weakening of the fibrous septum, leading to an unstable fat pad. Studies on the mechanism of action of polycaprolactone (PCL) collagen stimulators in the adipose layer are lacking.
Objectives
This research aimed to explore the effectiveness of PCL-based filler in enhancing the fibrous septum within adipose tissue, thereby facilitating collagen and elastin synthesis in the adipose layer, while also comparing the disparities in the process between juvenile and aged individuals.
Methods
A rat model was utilized to study subcutaneous fat implantation effects of PCL-based filler. Over 4 months, the impact on fibrous septum formation was evaluated with Masson's trichrome staining and immunostainings for Types I and III collagen, and a structural evaluation through scanning electron microscopy analysis. PCL-induced collagenization mechanisms were explored by quantitative polymerase chain reaction (qPCR). Elastin regeneration was examined with Elastica van Gieson (EVG) staining.
Results
Histological analysis demonstrated that PCL-based filler effectively stimulated collagen fiber formation in subcutaneous adipose tissue in both juvenile and aged rats. Immunostainings indicated significant promotion of Types I and III collagen regeneration, primarily within the interstitial spaces among adipocytes, as well as its confirmation at the genetic level through qPCR analysis. EVG staining further unveiled the role of PCL in promoting elastin production while mitigating age-related decline.
Conclusions
PCL-based filler enhanced fat septum regeneration and deposition, demonstrating a robust, age-independent response. These findings suggest PCL-based fillers as promising therapeutic agents for rejuvenating subcutaneous adipose tissue and enhancing skin volume and elasticity in cosmetic and reconstructive contexts.
Bone extracellular matrix (ECM) is comprised of organic and mineral components. Proteins, which are the primary constituents in the body that regulate all our actions, comprise the organic part of ECM. Collagen, a crucial and potent protein present in the body, mostly exists in supporting and connective tissues. Type I collagen is extensively used in the field of medicine because of its formation into fibrils consisting of triple helical polypeptide chains, which contribute to its remarkable mechanical properties. COL-V regulates the process of fibril production. There is conjecture that non-collagenous proteins may have a substantial impact on the regulation of hydroxyapatite mineral production, as well as the differentiation and attachment of cells. However, they possess several drawbacks such as restricted accessibility, high water solubility, and a lack of thorough understanding regarding their mechanism of action. Recently, multiple researchers have focused on striding each of these proteins individually, investigating their distinct characteristics and functions. Understanding the characteristics and dynamics of these proteins and their interactions with each other is crucial for the development of bone implants. ECM proteins can be employed either in their complete form or fragmented into peptides with specific sequences that will trigger the required reaction. For instance, collagen is commonly found in a variety of physical forms such as composites, sponges, membranes, films, solutions, gels, fibers, particles, powder, and so on. ECM proteins can also be utilized to enhance the biocompatibility of implants. This chapter will focus on the collagenous and non-collagenous proteins of the bone extracellular matrix.
In order for regenerative medicine strategies to achieve desired outcomes, the materials employed, mostly consisting of combinations of stem cells, growth factors, and scaffolds, must possess the ability to augment the regeneration of the original tissue or serve as a replacement for damaged tissue, functioning in a manner similar to the natural tissue. Due to variations in regeneration capabilities among different tissues, certain tissues may just require biologics and biomaterials, while others with partial regenerative capabilities necessitate the presence of cells, biomolecules, and biomaterials for regeneration. The ECM is accountable for preserving the flexibility and structural integrity of tissues. The structure undergoes constant remodeling in response to changes in the local pH levels, growth factors, and receptor abundance. The extracellular matrix (ECM) of bone and cartilage is unique, as it specifically caters to the distinct functional needs of these tissues. Collagen is the primary constituent of all extracellular matrices (ECMs). The bone extracellular matrix is predominantly composed of collagenous proteins, accounting for 90% of its makeup. The remaining 10% consists of non-collagenous proteins. Osteoblasts are accountable for the production of these proteins, primarily involved in cellular adhesion. Hydroxyapatite is the primary inorganic constituent of hard tissues. Collagen provides a structural base that aids in the deposition of hydroxyapatite during the mineralization of tissues. The extracellular matrix (ECM) of bone can be categorized into two components: organic and mineral. Each entity has distinct and individual attributes. It is important to consider that materials intended for insertion into bone tissue should replicate these characteristics. This chapter presents a thorough overview of the extracellular matrix of bones.
Gellan gum and collagen are two biomaterials that have been extensively studied for their potential use in wound healing and tissue engineering applications. Gellan gum is a biologically inert natural polymer that is increasingly favored as a biomaterial to form hydrogels. Collagen, on the other hand, is a major component of the extracellular matrix and is widely used in tissue engineering applications due to its biocompatibility and ability to promote cell adhesion and proliferation. In this review, the recent research will be discussed related to gellan gum and collagen, their properties, and their potential applications in wound healing and tissue engineering.
Collagens are biofunctional proteins that have been widely used in many fields, including biomedical, cosmetics, and skin care for their value in maintaining the integrity of cellular membranes. Collagens are also commonly consumed in foods and provide a source of protein and amino acids. As part of the safety assessment for this particular recombinant humanized type III (RHTypeIII) collagen produced by Komagataella phaffii SMD1168‐2COL3, a series of toxicological tests were conducted. This collagen has ≥ 90% amino acid sequence homology to bovine and porcine collagen. The RHTypeIII collagen showed no evidence of genotoxic potential in a battery of tests. It was not toxic in an acute oral study, with no effects at 10 g/kg BW. The RHTypeIII collagen was not developmentally toxic in Sprague Dawley (SD) rat, and the NOAEL was 4.5 g/kg BW/day. In a 90‐day oral gavage study in rats, there were no adverse findings observed; therefore, the high dose level (4.5 g/kg BW/day) was considered the NOAEL. The protein sequence was subjected to homology searches against the AllergenOnline database (sliding 80–amino acid windows and full sequence searches). From the 80‐amino acid alignment searches, 23 significant matches were identified (> 35% identity and E value < 1 × 10 ⁻⁷ ) to allergens of bovine, fish, anisakis, feverfew pollen, ragweed pollen, and wheat origin. Although matches were identified, further assessment of the in silico results combined with a literature review demonstrates that the risk of allergenic cross‐reactivity for this collagen is low. These results demonstrate RHTypeIII collagen is not toxic and unlikely to present a risk of allergy when used as a food ingredient.
This study endeavours to craft a potent topical facial mask using electrospun nanofibers. The nanofibers were carefully fabricated based on loading of N-acetylcysteine (NAC) onto electrospun marine collagen (MC), and poly (methyl methacrylate) (PMMA) nanofibers. Through precise adjustments of electrospinning parameters, a uniform array of nanoscale fibres with a smooth surface was achieved. The morphology and chemical structure configuration of nanofibers (NFs) were examined using SEM, FTIR, and XRD analyses. Furthermore, the cytotoxic impact was assessed on a human normal fibroblast cell line (BJ1), while protein levels were gauged using the Bradford dye-binding assay (Coomassie assay). Also, the antioxidant potential of various NFs scaffolds was evaluated through superoxide dismutase activity (SOD), catalase activity (CAT), and free radical scavenging assays. Controlled release of NAC from nanofibers was observed. Notably, PMMA/MC/NAC NFs exhibited notable antioxidant and strong antagonistic antimicrobial effects. After an 8-h treatment period, Staphylococcus epidermidis showed the highest percentage of biofilm reduction (96.46 ± 2.09 %) caused by this formula. Moreover, this formula effectively decreased the biofilm production of Candida glabrata (97.18 ± 0.48 %) and Klebsiella pneumoniae (96.38 ± 2.47 %) after a 12-h exposure period. These compelling findings put PMMA/MC/NAC NFs as promising candidate for facial masks and skincare formulations.
Collagen is the sole most profuse protein in the animal kingdom. It has been subjected to various studies from time immemorial. Its applications are numerous and have been extracted from various sources such as land animals (mainly bovine and porcine) and birds. Although collagen sources are abundant the outbreak of varied diseases among land animals posed a threat to its utilization in our daily life. Thus a probe for an alternative source began which in turn revealed the immense untapped marine source. The present article deals with a brief description of collagen its characteristics,chemistry,common extraction procedure, application in various fields and sources. A lot of studies have been carried out on various land animals, birds and marine organisms and this review sums up the work performed to date in a concise manner.
Collagen is the sole most profuse protein in the animal kingdom. It has been subjected to various studies from time immemorial. Its applications are numerous and have been extracted from various sources such as land animals (mainly bovine and porcine) and birds. Although collagen sources are abundant the outbreak of varied diseases among land animals posed a threat to its utilization in our daily life. Thus a probe for an alternative source began which in turn revealed the immense untapped marine source. The present article deals with a brief description of collagen its characteristics,chemistry,common extraction procedure, application in various fields and sources. A lot of studies have been carried out on various land animals, birds and marine organisms and this review sums up the work performed to date in a concise manner.
In the last two decades, many new peptides have been developed, and new knowledge on how peptides improve the skin has been uncovered. The spectrum of peptides in the field of cosmetics is continuously growing. This review summarizes some of the effective data on cosmeceutical peptides that work against intrinsic and extrinsic aging. Some peptides have been proven in their efficacy through clinical skin trials. Well-known and documented peptides like copper tripeptide are still under research to obtain more details on their effectiveness, and for the development of new treatments. Palmitoyl pentapeptide-4 and Carnosine are other well-researched cosmeceuticals. Additionally, there are many more peptides that are used in cosmetics. However, study results for some are sparse, or have not been published in scientific journals. This article summarizes topical peptides with proven efficacy in controlled in vivo studies.
Introduction: Bovine derived collagen membrane is usually and
regularly used as a temporary cover or dressing for the extra oral
wounds and for the burns on the body. It has wide applications
because of its usefulness and biocompatibility. This has provoked
us to do a study with the use of collagen membrane even for the
intraoral minor surgical defects.
Aim: The study was conducted to evaluate the clinical efficacy of
collagen membrane as a biological dressing material for intraoral
wounds, to check for haemostasis, pain control, granulation tissue
formation, rapid re-epithelialization and minimal contracture.
Materials and Methods: A total of 30 patients 19 male, 11
female were taken for excision of various intraoral lesions like
leukoplakia patches, mucocele, epulis growths, irritational fibroma,
frenectomy and the surgical defects were closed with collagen
membrane. Postoperatively healing was assessed by taking five
clinical parameters of Haemostasis, Pain, Granulation tissue,
Epithelialization, Contracture.
Results: Among 30 patients, haemostasis score was found to be
good in 28 cases, fair in two cases. Pain relief score was good
in seven cases, fair in 19 cases, poor in four cases. Granulation
tissue formation score was good in eight cases, fair in 13 cases,
poor in nine cases. Epithelialization score was good in 19 cases,
fair in seven cases, poor in four cases. Contracture score was
good in six cases, fair in 16 cases, poor in eight cases. Total score
of all the five parameters, which was rated as effectiveness score,
was calculated by using a standard scale. Final scoring was very
effective in six cases, effective in 20 cases, ineffective in four
cases.
Conclusion: Reconstituted bovine derived collagen membrane
used in our study was found to be an effective intraoral wound
dressing material for faster uneventful healing of intraorally also.
Collagen is the main structural protein of most hard and soft tissues in animals and the human body, which plays an important role in maintaining the biological and structural integrity of the extracellular matrix (ECM) and provides physical support to tissues. Collagen can be extracted and purified from a variety of sources and offers low immunogenicity, a porous structure, good permeability, biocompatibility and biodegradability. Collagen scaffolds have been widely used in tissue engineering due to these excellent properties. However, the poor mechanical property of collagen scaffolds limits their applications to some extent. To overcome this shortcoming, collagen scaffolds can be cross-linked by chemical or physical methods or modified with natural/synthetic polymers or inorganic materials. Biochemical factors can also be introduced to the scaffold to further improve its biological activity. This review will summarize the structure and biological characteristics of collagen and introduce the preparation methods and modification strategies of collagen scaffolds. The typical application of a collagen scaffold in tissue engineering (including nerve, bone, cartilage, tendon, ligament, blood vessel and skin) will be further provided. The prospects and challenges about their future research and application will also be pointed out.
Collagen is the main protein of the connective tissue and its molecule is formed by three polypeptide strands, named alpha chains. The most common motifs in the amino acid sequence of collagen are Gly-Pro-X and Gly-X-Hyp. Collagen can be extracted from a variety of organisms. The use of cattle as the main source for collagen has been reconsidered because of the bovine spongiform encephalopathy and transmissible spongiform encephalopathy, while porcine origin collagen is increasingly rejected for religious reasons. One alternative is the extraction of collagen from marine sources. Sponges, jellyfishes, squids, octopuses, cuttlefishes and fish offal (bones, skin, scales and fins) can serve as an alternative source of collagen. Nowadays there is a high biotechnological interest of marine collagenous, as witnessed by a wide pattern of applications in biomedicine, food science, and cosmetics.
Skin, the main barrier to the external environment, is subject to deterioration caused by dermatological disorders, environmental conditions and the intrinsic ageing process. This damage to both structure and function may be accelerated by smoking, alcohol consumption and chronic sun exposure (extrinsic components). All these factors may lead to the formation of wrinkles, the appearance of brown spots and skin thickening. One effective strategy to managing the skin ageing process is adopting a healthy nutritional approach to life, maintaining a balanced diet and a good supply of food supplements. This can restore the homeostasis of macro and micronutrients and support the physiology of cells and tissues in the skin. Hydrolysed collagen, an increasingly popular nutraceutical, is composed of low molecular weight small peptides, which are easily digestible, absorbed and distributed in the human body. Numerous clinical trials have now been performed showing the efficacy and benefits of collagen peptides on skin properties, such as hydration, elasticity and reduction of wrinkles. As a result, hydrolysed collagen can be considered an important weapon in the everyday fight against skin ageing.
Collagens are the most abundant high molecular weight proteins in both invertebrate and vertebrate organisms, including mammals, and possess mainly a structural role, existing different types according with their specific organization in distinct tissues. From this, they have been elected as one of the key biological materials in tissue regeneration approaches. Also, industry is constantly searching for new natural sources of collagen and upgraded methodologies for their production. The most common sources are from bovine and porcine origin, but other ways are making their route, such as recombinant production, but also extraction from marine organisms like fish. Different organisms have been proposed and explored for collagen extraction, allowing the sustainable production of different types of collagens, with properties depending on the kind of organism (and their natural environment) and extraction methodology. Such variety of collagen properties has been further investigated in different ways to render a wide range of applications. The present review aims to shed some light on the contribution of marine collagens for the scientific and technological development of this sector, stressing the opportunities and challenges that they are and most probably will be facing to assume a role as an alternative source for industrial exploitation.
Purpose
Type VI collagen is a primary component of the extracellular matrix of many connective tissues. It can form distinct aggregates depending on tissue structure, chemical environment, and physiology. In the current study we examine the ultrastructure and mode of aggregation of type VI collagen molecules in the human trabecular meshwork.
Methods
Trabecular meshwork was dissected from donor human eyes, and three-dimensional transmission electron microscopy of type VI collagen aggregates was performed.
Results
Electron-dense collagen structures were detected in the human trabecular meshwork and identified as collagen type VI assemblies based on the three-dimensional spatial arrangement of the type VI collagen molecules, the 105-nm axial periodicity of the assemblies themselves, and their characteristic double bands, which arose from the globular domains of the type VI collagen molecules. Sulfated proteoglycans were also seen to associate with the assemblies either with the globular domain or the inner rod-like segments of the tetramers.
Conclusions
No extended structural regularity in the organization of type VI collagen assemblies within the trabecular meshwork was evident, and the lateral separation of the tetramers forming the assemblies varied, as did the angle formed by the main axes of adjacent tetramers. This is potentially reflective of the specific nature of the trabecular meshwork environment, which facilitates aqueous outflow from the eye, and we speculate that extracellular matrix ions and proteins might prevent a more tight packing of type VI collagen tetramers that form the assemblies.
Skin aging is a complex biological process influenced by a combination of endogenous or intrinsic and exogenous or extrinsic factors. Because of the fact that skin health and beauty is considered one of the principal factors representing overall "well-being" and the perception of "health" in humans, several anti-aging strategies have been developed during the last years. It is the intention of this article to review the most important anti-aging strategies that dermatologists have nowadays in hand, including including preventive measurements, cosmetological strategies, topical and systemic therapeutic agents and invasive procedures.
Jellyfish collagen (JC) was extracted from jellyfish umbrella and hydrolyzed to prepare jellyfish collagen hydrolysate (JCH). The effects of JC and JCH on UV-induced skin damage of mice were evaluated by the skin moisture, microscopic analyses of skin and immunity indexes. The skin moisture analyses showed that moisture retention ability of UV-induced mice skin was increased by JC and JCH. Further histological analysis showed that JC and JCH could repair the endogenous collagen and elastin protein fibers, and could maintain the natural ratio of type I to type III collagen. The immunity indexes showed that JC and JCH play a role in enhancing immunity of photoaging mice in vivo. JCH showed much higher protective ability than JC. These results suggest that JCH as a potential novel antiphotoaging agent from natural resources.
Collagens require the hydroxylation of proline (Pro) residues in their triple-helical domain repeating sequence Xaa-Pro-Gly to function properly as a main structural component of the extracellular matrix in animals at physiologically relevant conditions. The regioselective proline hydroxylation is catalyzed by a specific prolyl 4-hydroxylase (P4H) as a posttranslational processing step.
A recombinant human collagen type I α-1 (rCIα1) with high percentage of hydroxylated prolines (Hyp) was produced in transgenic maize seeds when co-expressed with both the α- and β- subunits of a recombinant human P4H (rP4H). Germ-specific expression of rCIα1 using maize globulin-1 gene promoter resulted in an average yield of 12 mg/kg seed for the full-length rCIα1 in seeds without co-expression of rP4H and 4 mg/kg seed for the rCIα1 (rCIα1-OH) in seeds with co-expression of rP4H. High-resolution mass spectrometry (HRMS) analysis revealed that nearly half of the collagenous repeating triplets in rCIα1 isolated from rP4H co-expressing maize line had the Pro residues changed to Hyp residues. The HRMS analysis determined the Hyp content of maize-derived rCIα1-OH as 18.11%, which is comparable to the Hyp level of yeast-derived rCIα1-OH (17.47%) and the native human CIa1 (14.59%), respectively. The increased Hyp percentage was correlated with a markedly enhanced thermal stability of maize-derived rCIα1-OH when compared to the non-hydroxylated rCIα1.
This work shows that maize has potential to produce adequately modified exogenous proteins with mammalian-like post-translational modifications that may be require for their use as pharmaceutical and industrial products.
Collagen is the most widely distributed class of proteins in the human body. The use of collagen-based biomaterials in the field of tissue engineering applications has been intensively growing over the past decades. Multiple cross-linking methods were investigated and different combinations with other biopolymers were explored in order to improve tissue function. Collagen possesses a major advantage in being biodegradable, biocompatible, easily available and highly versatile. However, since collagen is a protein, it remains difficult to sterilize without alterations to its structure. This review presents a comprehensive overview of the various applications of collagen-based biomaterials developed for tissue engineering, aimed at providing a functional material for use in regenerative medicine from the laboratory bench to the patient bedside.
Bridging nerve gaps with suitable grafts is a major clinical problem. The autologous nerve graft is considered to be the gold standard, providing the best functional results; however, donor site morbidity is still a major disadvantage. Various attempts have been made to overcome the problems of autologous nerve grafts with artificial nerve tubes, which are “ready-to-use” in almost every situation. A wide range of materials have been used in animal models but only few have been applied to date clinically, where biocompatibility is an inevitable prerequisite. This review gives an idea about artificial nerve tubes with special focus on their biocompatibility in animals and humans.
The collagens represent a family of trimeric extracellular matrix molecules used by cells for structural integrity and other functions. The three alpha chains that form the triple helical part of the molecule are composed of repeating peptide triplets of glycine-X-Y. X and Y can be any amino acid but are often proline and hydroxyproline, respectively. Flanking the triple helical regions (i.e., Col domains) are non-glycine-X-Y regions, termed non-collagenous domains. These frequently contain recognizable peptide modules found in other matrix molecules. Proper tissue function depends on correctly assembled molecular aggregates being incorporated into the matrix. This review highlights some of the structural characteristics of collagen types I-XXVIII.
The most common form of chronic arthritis is osteoarthritis (OA) with prevalence as high as 80% after age 75 (Arden and Nevitt, 2006). The incidence of OA is expected to increase as the population ages, increasing the socioeconomic burden of OA. Despite the signifi cant burden of this disease, no drug has been identifi ed that can effectively modify disease progression (Moskowitz and Hooper, 2005; Abadie et al. 2004). However, slowing disease progress and improvement in quality of life may be achieved by behavioral modifi cations, such as weight loss and exercise. Many patients with early OA will progress to disability and joint replacement. Physical examination and radiographic studies are relatively poor means for detecting disease early or predicting progression. Therefore, identifi cation of factors to facilitate early OA diagnosis and prognosis is a major focus of current OA research (Lohmander and Felson, 2004; Lohmander, 2004; Garnero and Delmas, 2003).
The 2 A crystal structure reported here of the collagen-like model peptide, T3-785, provides the first visualization of how the sequence of collagen defines distinctive local conformational variations in triple-helical structure.
The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified so far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. This review focuses on the distribution and function of various collagen types in different tissues. It introduces their basic structural subunits and points out major steps in the biosynthesis and supramolecular processing of fibrillar collagens as prototypical members of this protein family. A final outlook indicates the importance of different collagen types not only for the understanding of collagen-related diseases, but also as a basis for the therapeutical use of members of this protein family discussed in other chapters of this issue.
Dystrophic epidermolysis bullosa (DEB) is a family of inherited mechano-bullous disorders that are caused by mutations in the type VII collagen gene and for which ex vivo gene therapy has been considered. To develop a simpler approach for treating DEB, we evaluated the feasibility of protein-based therapy by intradermally injecting human recombinant type VII collagen into mouse skin and a DEB human skin equivalent transplanted onto mice. The injected collagen localized to the basement membrane zone of both types of tissues, was organized into human anchoring fibril structures and reversed the features of DEB disease in the DEB skin equivalent.
Objectives
This study was undertaken to identify the types of collagen fibrils in the extracellular matrix of the human vocal fold lamina propria.
Methods
Human vocal folds were obtained from 3 autopsy cases less than 65 years of age. The vocal fold specimens were labeled by primary antibodies of anti-type I and anti-type III collagens, and then by secondary antibody conjugated with 15 nm colloidal gold. The specimens were observed with a scanning electron microscope. Secondary electron imaging and backscatter electron imaging of high-resolution field emission scanning electron microscopy were used to detect gold particles indicating immunolabeling.
Results
Type III collagen-labeling gold particles were abundant on the fibrils constructing collagenous fibers, whereas type I collagen-labeling gold particles were sparsely present on fibrils in collagenous fibers. A few reticular fibers were labeled by both collagen type I and collagen type III.
Conclusions
The results suggest that collagen type I coexists with collagen type III in fibrils of both collagenous fibers and reticular fibers.
Western beauty standards play an important role in our society, being a pattern to follow by millions of young people. It is due to the presence of these certain standards of beauty that the numbers of cases related to eating disorders have increased in recent years. Many factors contribute to the manifestation of eating disorders, among the most important are those that through cultural practices and culture that can transmit messages influential manifestation of anorexia. The objective of this research is to identify what is the relationship between beauty standards that are present in our cultural practices and habitus, and symbolic violence with which these diseases manifest, in order to identify whether are decisive in manifesting anorexia in young of Panama. To carry out the study identification space to the village of Bellavista, located in Panama City, Panama was delimited. Both, qualitative and quantitative methodology are employed through interviews, focus groups and surveys respectively.
Biochemistry of Collagens, Laminins, and Elastin: Structure, Function, and Biomarkers provides a comprehensive introduction to collagen and structural proteins. Type I collagen is one of the most abundant molecules in the body, playing essential roles in different tissues, particularly bone and skin. A key aspect of type I collagen is its post-translational modifications which are essential for correct synthesis and structural integrity of collagens, for tissue-specific functionality, as well as for application as biomarkers of different pathologies. This volume summarizes current data on key structural proteins (collagens, laminins and elastin), reviews how these molecules affect pathologies, and describes selected modifications of proteins that result in altered signaling properties of the original extracellular matrix component. Further, it discusses the novel concept that an increasing number of components of the ECM harbor cryptic signaling functions that may be viewed as endocrine functions. Additionally, it highlights how this knowledge can be exploited to modulate fibrotic disease. Provides a comprehensive introduction to collagen and structural proteins Provides insight into emerging analytical technologies that can detect biomarkers of extracellular matrix degradation Includes a chapter dedicated to the biomarkers of structural proteins Contains insights into the biochemical interactions and changes to structural composition of proteins in disease states.
This review reports recent advances in the versatile application of collagen. Collagen materials have attracted great attention because they exhibit properties required in cosmetic preparations, in the biomedical field, and in the tanning industry leading to leather production. Herein, the structure and application of collagen are discussed in general, and detailed examples are also drawn from scientific literature and practical work.
Collagen is an important biomaterial in medical applications due to its special characteristics, such as biodegradability and weak antigenicity. Thus collagen, as a new type of biomaterial, has been used in drug delivery systems and tissue engineering. Collagen is capable of being prepared into cross-linked compacted solids or into lattice-like gels. Resorbable forms of collagen have been used to dress oral wounds, for closure of graft and extraction sites, and to promote healing. Collagen-based membranes also have been used in periodontal and implant therapy as barriers to prevent epithelial migration and allow cells with regenerative capacity to repopulate the defect area. It has been hypothesized that membrane regenerative techniques facilitate the natural biological potential by creating a favorable environment for periodontal and peri-implant regeneration. Due to the enormous potential of collagen-based regenerative barriers, clinicians may benefit from a review of potential applications of implantable collagen and knowledge of collagen preparation and membrane types as well as from as awareness of the functional and degradation properties of those materials.
Collagen is the most abundant natural protein found in living systems. While there is a whole family of different collagen types, each differing in sequence, the properties that make this protein so attractive as the building blocks for medical devices, are reflected largely by the unique fibrillar structure of the molecule, as well as defined functional regions that interact with the surrounding cells and other matrix components. As a commercial medical product, collagen can be part of the natural tissue used in the device, or it can be fabricated as a reconstituted product from animal or recombinant sources. Both types of uses have distinct properties that convey advantages and disadvantages to the end product. This review examines the chemistry and biology of collagen and describes some well-documented examples of collagen-based medical devices produced in one or other of these formats.
-INTRODUCTION TO BIOMATERIALS. -THE STRUCTURE OF SOLIDS. -CHARACTERIZATION OF MATERIALS-I. -CHARACTERIZATION OF MATERIALS-II: ELECTRICAL, OPTICAL, X-RAY ABSORPTION, ACOUSTIC, ULTRASONIC, ETC.-METALLIC IMPLANT MATERIALS. -CERAMIC IMPLANT MATERIALS. -POLYMERIC IMPLANT MATERIALS. -COMPOSITES AS BIOMATERIALS. -STRUCTURE-PROPERTY RELATIONSHIPS OF BIOLOGICAL MATERIALS. -TISSUE RESPONSE TO IMPLANTS. -SOFT TISSUE REPLACEMENT I: SUTURES, SKIN, AND MAXILLOFACIAL IMPLANTS. -SOFT TISSUE REPLACEMENT II: BLOOD INTERFACING IMPLANTS. -HARD TISSUE REPLACEMENT I: LONG BONE REPAIR. -HARD TISSUE REPLACEMENT-II: JOINTS AND TEETH. -TRANSPLANTS. -BIODEGRADABLE MATERIALS FOR TISSUE ENGINEERING. -APPENDICES.
Collagen is a major component of the extracellular matrix and plays a wide variety of important roles in blood clotting, healing, and tissue remodeling. Natural, animal derived, collagen is used in many clinical applications but concerns exist with respect to its role in inflammation, batch-to-batch variability, and possible disease transfection. Therefore, development of synthetic nanomaterials that can mimic the nanostructure and properties of natural collagen has been a heavily pursued goal in biomaterials. Previously, we reported on the design and multihierarchial self-assembly of a 36 amino acid collagen mimetic peptide (KOD) that forms nanofibrous triple helices that entangle to form a hydrogel. In this report, we utilize this nanofiber forming collagen mimetic peptide as a synthetic biomimetic matrix useful in thrombosis. We demonstrate that nanofibrous KOD synthetic collagen matrices adhere platelets, activate them (indicated by soluble P-selectin secretion), and clot plasma and blood similar to animal derived collagen and control surfaces. In addition to the thrombotic potential, THP-1 monocytes incubated with our KOD collagen mimetic showed minimal proinflammatory cytokine (TNF-α or IL-1β) production. Together, the data presented demonstrates the potential of a novel synthetic collagen mimetic as a hemostat.
Collagen is the most abundant protein in the human body. Of the 25 types of collagen known, fibril-forming collagen is the main component in many tissues such as tendons, cartilage and bone to provide the structural framework and the strength of tissues. Fibril-forming collagen is characterized by a hierarchical assembly of substructures. In this hierarchical arrangement, collagen molecules consisting of three polypeptide chains assemble into fibrils with diameters in the range of 10 - 500 nm and the fibrils further assemble into fibers. Due to the limitations in performing mechanical testing on the nanometer and micrometer scale, only very recently studies have been initiated on the mechanical properties of sub-structures like collagen fibrils and the respective influence of each level of the hierarchical structure on the overall mechanical properties of tissue. Next to collagen, many tissues for instance blood vessels contain elastic fibers which are mainly responsible for providing elasticity to tissues and organs in vertebrates. The elastic fibers contain elastin and fibrillin-microfibrils. The role of fibrillin-microfibrils in the mechanical properties of elastic fibers has been a debate for years.
It was the aim of this work to explore the relationship between the mechanical properties and structure of collagen fibrils and elastic fibers, which also provides a better insight in the micromechanical behavior of tissues. To achieve this aim, the mechanical properties of single collagen fibrils and elastic fibers were determined using newly developed AFM-based micro-mechanical bending tests and micro-tensile tests. Tensile properties, shear related properties and viscoelastic behavior of single collagen fibrils at ambient conditions and immersed in buffer were determined. Furthermore, the influence of different cross-linking agents on the mechanical properties of collagen fibrils was studied. The mechanical properties of these cross-linked collagen fibrils provided insight into the existence of microfibrils, an intermediate structure between collagen molecules and fibrils. In a separate set of experiments, the mechanical properties of elastic fibers devoid of or containing fibrillin-microfibrils were determined to evaluate the role of fibrillin-microfibrils in the mechanical properties of elastic fibers.
Extracellular matrix (ECM) based scaffolds, through their inherent bioactivity and molecular recognition signals, provide the ideal substrate for tissue engineering and regenerative applications. Collagen, the most abundant ECM protein, has proven itself to be a very versatile material with applications in many fields including the leather and food industries, cosmetics, drug delivery and tissue engineering. However, doubts persist about the optimal source of collagen for tissue engineering applications, given possible immunogenicity and disease transmission associated with animal sources and reduced bioactivity and availability of recombinant technologies. In this special edition, an attempt is made to elucidate the advantages of plant-derived human recombinant collagen and its applications in tissue engineering, particularly skin and wound healing. While results are promising, the widespread use of animal derived collagen means that recombinant technologies may find applications in niche areas.
Prolidase deficiency is a rare, autosomal recessively inherited disorder in which deficient activity of prolidase results in a massive urinary excretion of X-Pro and X-Hyp dipeptides derived from generalized protein breakdown. The chapter includes discussions on the clinical features of the disorder, inheritance and prevalence, diagnosis, prognosis and management.
Collagen is the principal structural protein present in the skin, tendon and bone of the vertebrate body. Ten different vertebrate
collagens have been identified, of which the dominant collagen is type I. Interest in collagen as a biomaterial is due to
its low immunogenicity and high biocompatibility. Collagen has diverse general and biomedical applications and is also a common
constituent of many cosmetic and food products in the form of gelatin. This paper discusses the use of collagen in the fields
of medicine and biotechnology, as well as in the cosmetic and pharmaceutical industry.
Collagen, the most abundant protein in vertebrates, is a useful biomaterial in pharmaceutical and medical industries. So far, most collagen has been extracted from animals and cadavers. Herein, we suggest human adipose tissue, which is routinely abandoned after liposuction, as a plentiful source of human collagen. In this study, human collagen was obtained from adipose tissue through two successive major steps: (i) extraction of the extracellular matrix (ECM) by pulverization, centrifugation, alkaline, and alcohol treatment; (ii) isolation of collagen from ECM by pepsin treatment in dilute acetic acid. The purified human adipose-derived collagen was characterized by Fourier transform infrared spectroscopy, polyacrylamide gel electrophoresis, amino acid analysis, and circular dichroism spectroscopy. The extracted collagen showed a typical triple helix structure, good thermal stability due to abundant imino acids, and high solubility at acidic pH. The collagen greatly facilitated the adhesion and proliferation of human adipose-derived stem cells and normal human dermal fibroblasts on polystyrene plates. These results suggest that human adipose tissue obtained by liposuction can provide human collagen for use in cosmetics, pharmaceutics, and medicine.
Collagen constitutes one-third of the human proteome, providing mechanical stability, elasticity, and strength to organisms. Normal type I collagen is a heterotrimer triple-helical molecule consisting of two α-1 chains and one α-2 chain. The homotrimeric isoform of type I collagen, which consists of three α-1 chains, is only found in fetal tissues, fibrosis, and cancer in humans. A mouse model of the genetic brittle bone disease, osteogenesis imperfect, oim, is characterized by a replacement of the α-2 chain by an α-1 chain, resulting also in a homotrimer collagen molecule. Experimental studies of oim mice tendon and bone have shown reduced mechanical strength compared to normal mice. The relationship between the molecular content and the decrease in strength is, however, still unknown. Here, fully atomistic simulations of a section of mouse type I heterotrimer and homotrimer collagen molecules are developed to explore the effect of the substitution of the α-2 chain. We calculate the persistence length and carry out a detailed analysis of the structure to determine differences in structural and mechanical behavior between hetero- and homotrimers. The results show that homotrimer persistence length is half of that of the heterotrimer (96 Å vs. 215 Å), indicating it is more flexible and confirmed by direct mechanical testing. Our structural analyses reveal that in contrast to the heterotrimer, the homotrimer easily forms kinks and freely rotates with angles much larger than heterotrimer. These local kinks may explain the larger lateral distance between collagen molecules seen in the fibrils of oim mice tendon and could have implications for reducing the intermolecular cross-linking, which is known to reduce the mechanical strength.
During adipogenic differentiation human mesenchymal stem cells (hMSC) produce collagen type IV. In immunofluorescence staining differentiating hMSCs started to express collagen type IV when Oil Red O-positive fat droplets appeared intracellularly. Quantitative real time-polymerase chain reaction confirmed progressive increase of collagen type IV α1 and α2 mRNA levels over time, 18.6- and 12.2-fold by day 28, respectively, whereas the copy numbers of α3-α6 mRNAs remained rather stable and low. Type IV collagen was in confocal laser scanning microscopy seen around adipocytes, where also laminins and nidogen were found, suggesting pericellular deposition of all key components of the fully developed basement membrane. Immunofluorescence staining of matrix metalloproteinase-2 (MMP-2, 72 kD type IV collagenase, gelatinase A) and MMP-9 (92 kD type IV collagenase, gelatinase B) disclosed only faint staining of MSCs, but MMP-9 was strongly induced during adipogenesis, whereas MSC supernatants disclosed in zymography pro-MMP-2 and faint pro-MMP-9 bands, which increased over time, with partial conversion of pro-MMP-2 to its active 62 kD form. Differentiation was associated with increasing membrane type 1-MMP/MMP-14 and tissue inhibitor of metalloproteinase-2 (TIMP-2) staining, which may enable participation of type IV collagenases in basement membrane remodelling via ternary MT1-MMP/TIMP-2/MMP-2 or -9 complexes, focalizing the fully active enzyme to the cell surface. MMP-9, which increased more in immunofluorescence staining, was perhaps preferentially bound to cell surface and/or remodelling adipocyte basement membrane. These results suggest that upon MSC-adipocyte differentiation collagen type IV synthesis and remodelling become necessary when intracellular accumulation of fat necessitates a dynamically supporting and instructive, partly denatured adipogenic pericellular type IV collagen scaffold.
Collagens are the most abundant proteins in mammals. The collagen family comprises 28 members that contain at least one triple-helical domain. Collagens are deposited in the extracellular matrix where most of them form supramolecular assemblies. Four collagens are type II membrane proteins that also exist in a soluble form released from the cell surface by shedding. Collagens play structural roles and contribute to mechanical properties, organization, and shape of tissues. They interact with cells via several receptor families and regulate their proliferation, migration, and differentiation. Some collagens have a restricted tissue distribution and hence specific biological functions.
The present investigation evaluated arthritic pain in horses receiving daily placebo, undenatured type II collagen (UC-II) at 320, 480, or 640 mg (providing 80, 120, and 160 mg active UC-II, respectively), and glucosamine and chondroitin (5.4 and 1.8 g, respectively, bid for the first month, and thereafter once daily) for 150 days. Horses were evaluated for overall pain, pain upon limb manipulation, physical examination, and liver and kidney functions. Evaluation of overall pain was based upon a consistent observation of all subjects during a walk and a trot in the same pattern on the same surface. Pain upon limb manipulation was conducted after the walk and trot. It consisted of placing the affected joint in severe flexion for a period of 60 sec. The limb was then placed to the ground and the animal trotted off. The response to the flexion test was then noted with the first couple of strides the animal took. Flexion test was consistent with determining clinically the degree of osteoarthritis in a joint. Horses receiving placebo showed no change in arthritic condition, while those receiving 320 or 480 or 640 mg UC-II exhibited significant reduction in arthritic pain (P < 0.05). UC-II at 480 or 640 mg dose provided equal effects, and therefore, 480 mg dose was considered optimal. With this dose, reduction in overall pain was from 5.7 +/- 0.42 (100%) to 0.7 +/- 0.42 (12%); and in pain upon limb manipulation from 2.35 +/- 0.37 (100%) to 0.52 +/- 0.18 (22%). Although glucosamine and chondroitin treated group showed significant (P < 0.05) reduction in pain compared with pretreated values, the efficacy was less compared with that observed with UC-II. In fact, UC-II at 480 or 640 mg dose was found to be more effective than glucosamine and chondroitin in arthritic horses. Clinical condition (body weight, body temperature, respiration rate, and pulse rate), and liver (bilirubin, GGT, and ALP) and kidney (BUN and creatinine) functions remained unchanged, suggesting that these supplements were well tolerated.
Soft tissue grafting is often required to correct intraoral mucosal deficiencies. Autogenous grafts have disadvantages including an additional harvest site with its associated pain and morbidity and, sometimes, poor quality and limited amount of the graft. Porcine collagen matrices have the potential to be helpful for grafting of soft tissue defects.
Thirty consecutive patients underwent intraoral grafting to re-create missing soft tissue. Defects ranged in size from 50 to 900 mm(2). Porcine collagen matrices were used to reconstruct missing tissue. Indications included preprosthetic (22), followed by tumor removal (5), trauma (2), and release of cheek ankylosis (1).
The primary efficacy parameters evaluated were the degree of lateral and/or alveolar extension and the evaluation of re-epithelialization and shrinkage of the grafted area. Overall, the percentage of shrinkage of the graft was 14% (range, 5%-20%). The amount of soft tissue extension averaged 3.4 mm (range, 2-10 mm). The secondary efficacy parameters included hemostatic effect, pain evaluation, pain and discomfort, and clinical evaluation of the grafted site. All patients reported minimal pain and swelling associated with the grafted area. No infections were noted.
This porcine collagen matrix provides a biocompatible surgical material as an alternative to an autogenous transplant, thus obviating the need to harvest soft tissue autogenous grafts from other areas of the oral cavity.
The effect of type IX on in vitro fibrillogenesis of type II collagen indicated that, while not preventing fibrillogenesis, the presence of type IX collagen reduced the size of the type II fibre aggregates. This observation is consistent with the in vivo localisation studies of type IX collagen. Using the immunogold labelling technique, type IX collagen was shown to be located evenly on small fibrils which occur at higher concentration closer to the cell. Therefore type IX collagen may function as a regulator of fibre diameter in articular cartilage.
We investigated the efficacy of polyethylene glycol (PEG) for effective and reproducible concentration of urinary type IV collagen prior to measurement by enzyme immunoassay (EIA). Human placental type IV collagen at low concentrations (5 and 10μg/L) and urinary type IV collagen were readily precipitated by PEG-4000 added at a concentration of about 150 g/L in the presence of 0·5 g/L γ-globulin. Type IV collagen measurement by EIA from PEG-concentrated urine samples showed complete recovery and good reproducibility. Analysis of size distribution by Sephacryl S-300HR gel chromatography and Western blotting following polyacrylamide gel electrophoresis confirmed that type IV collagen in PEG-concentrated urine samples was of high molecular weight comparable to that of human placental type IV collagen. After PEG concentration, type IV collagen was detectable by EIA even in the urine of healthy subjects. Significantly higher concentrations of urinary type IV collagen were found in 30 diabetic patients with nephropathy than in 20 healthy subjects [99·5 (8·9)μg/L, mean (SEM) versus 21·4 (2·6)μg/L, P<0·0001].
Thus, urinary type IV collagen can be measured effectively by EIA following concentration with PEG. This method has potential for the assessment of the progression of diabetic nephropathy.
Prion diseases are uncommon fatal neurodegenerative disorders that have gained scientific importance as a result of the emergence of new forms of these diseases in both animals and humans. Prions appear to be composed principally or entirely of abnormal isoforms of a host-encoded glycoprotein. There is substantial scientific evidence to support the notion that bovine spongiform encephalopathy ("mad cow disease") has affected humans. Recent studies have demonstrated that prions can adhere easily to metal surfaces, and normal sterilization procedures are not likely to completely inactivate them. Iatrogenic transmission of prion diseases, such as Creutzfeldt-Jakob disease, was recognized after corneal transplantations, dura mater grafts, neurosurgical procedures, and the use of human hormones (growth hormone and gonadotropin). Although bovine collagen has long been recognized as a safe and biocompatible material, dermatologists should be aware of the theoretical potential for prion transmission when materials from bovine origin and products obtained from cultured cells fed with fetal or newborn calf serum are used.
The collagen family includes several large transcripts, usually exceeding 1000 aminoacid residues per single chain. As a group, they make up 1/3 of all the protein of the body and are responsible for modelling the framework of connective tissues; individually, they show both a wide variety and a complex hierarchy of mutual interactions, and form a range of functional aggregates including a variety of fibrils, microfibrils and basal membranes. Of the collagens, the fibril-forming types (i.e. the types I, II III, V and XI) are the most abundant and the most extensively studied.
To characterize the function of type XIII collagen, a transmembrane protein occurring at cell adhesion sites, we generated transgenic mice overexpressing it. High transgene expression was detected in cartilage and bone. The overexpression mice developed an unexpected skeletal phenotype marked by a massive increase in bone mass caused by increased bone formation rather than impaired resorption.
Type XIII collagen is a type II transmembrane protein that is expressed in many tissues throughout development and adult life. It is located in focal adhesions of cultured fibroblasts and other cells and in the adhesive structures of tissues. To further characterize the function of this protein, we generated transgenic mice overexpressing it. High transgene expression was detected in cartilage and bone in locations also containing the endogenous protein.
Col13a1 5'-flanking sequences were tested for their efficiencies to drive gene expression. Skeletal tissues of transgenic mice and wildtype littermates were compared using histological, immunohistochemical, and bone histomorphometrical analyses. Bone formation rate was measured by tetracycline double-labeling. Osteoclast number and resorption activity were determined using standard methods. RNA samples from transgenic and wildtype femurs were analyzed by Northern blotting and quantitative RT-PCR.
There was no defect in early skeletal development, but the high bone mass phenotype became apparent in heterozygous mice at the age of 3-4 weeks. The changes were most noticeable in proximal long bones but were also detectable in calvarial bones. The cortical bone cross-sectional area and the volumetric BMD were highly increased, but the bone marrow was well formed. Histological and histomorphometric analysis showed that trabecular bone volume was not significantly altered. Because of the normal epiphyseal growth plates, the longitudinal growth was not affected. Bone formation rate was several times higher in the overexpression mice than in their normal littermates, whereas the osteoclast number and resorption activity were normal. RNA analysis revealed increased expression in the transcription factor Runx2 and IGF-II, both known to be involved in bone biology.
Overexpression of type XIII collagen in skeletal tissues leads postnatally to an abnormally high bone mass caused by increased bone formation rather than impaired resorption. The findings suggest that type XIII collagen has an important role in bone modeling, and in particular, it may have a function in coupling the regulation of bone mass to mechanical use.
Absence or segmental distribution of the alpha5(IV) collagen chain along the epidermal basement membrane (EBM) is diagnostic of X-linked Alport syndrome (X-AS), but the typical morphologic alterations usually observed along the glomerular basement membrane (GBM) are lacking. However, several differences in protein composition exist between GBM and EBM, and such differences could account for a different phenotype with the same genetic defect. Type VII collagen is one of the major collagenous components of the EBM; the purpose of this study was to investigate the modifications of protein synthesis and expression of type VII collagen in the skin of patients with X-AS.
The distribution of type VII collagen has been studied in 15 skin biopsies (10 from X-AS patients and 5 controls) by means of electron microscopy, immunofluorescence and confocal microscopy; type VII collagen mRNA expression was also measured by RT-PCR on the same skin fragments.
Protein and mRNA amounts for type VII collagen were significantly higher in skin samples from X-AS patients than in controls (P < 0.001); highest values were in cases in which alpha5(IV) was completely absent.
Our results indicate that lack of alpha5(IV) molecule significantly alters the assembly of extracellular matrix molecules other than alphax(IV) chains also at the EBM level. We suggest that the increased synthesis and deposition of type VII collagen is likely to balance the absence of stabilizing activity normally exerted by alpha5(IV).