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ACE inhibitors generated from food proteins have recently become the most well-known subclass of bioactive peptides, and their bio-functionality can be a potential alternative to natural bioactive food components and synthetic drugs. The bioactivities of Acrochaetium sp., the red alga used in this investigation, have never been reported before. Scr...
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Angiotensin-I Converting Enzyme (ACE) plays a pivotal role in regulating hypertension. Inhibition of ACE by potent inhibitors is an excellent approach to treating high blood pressure and related cardiac ailments. Dietary proteins are a good source of bioactive peptides with a broad spectrum of pharmacological activities. An attempt has been made in...
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... The P5 fraction showed the strongest antibacterial activity against four test strains of bacteria, including both Gram-positive and Gram-negative types, within the concentration range of 1 to 4 mg/mL, after the hydrolysate was fractionated into (Gao et al., 2021a;Mun et al., 2024) multiple fractions for their investigation (Song et al., 2020b). Windarto et al. (2022) studied the red algae Acrochaetium sp. for new peptides that inhibited the angiotensin-I converting enzyme. They utilised strong CEC resins (off-line SCX chromatography) to fractionate the protein hydrolysates of Acrochaetium sp. ...
... The fraction obtained from the 20% elution solution showed the strongest ACE inhibitory activity, according to ACE inhibition experiments. The peptide sequence was identified as VGGSDLQAL (VL-9) (Windarto et al., 2022). Pujiastuti et al. (2017) fractionated enzymatic hydrolysates of soft-shelled turtle yolk proteins into seven fractions using strong CEC resin (Wang resin, Cleo Salus). ...
Bioactive peptides produced from food proteins have garnered significant attention for their potential as functional foods in recent times. Applications for bioactive peptides have advanced rapidly due to the continuous improvement of fractionation techniques. Studies have shown that the process of fractionation can affect the activity of bioactive peptides, resulting in certain fractions exhibiting notably greater activities than others. This implies that fractionation procedures can be used to develop more highly valued and active bioactive peptide molecules. These fractionated peptides provide several health benefits, such as anti-inflammatory, antibacterial, anticancer, antioxidant, and antidiabetic properties. They are crucial to the production of functional foods. This paper summarises the most recent advancements in the field of bioactive peptide fractionation techniques, with a focus on membrane, isoelectric, and chromatography separation methods. It investigates how different fractionation methods impact the bioactivity of bioactive peptides and highlights the use of multiple combined methods. By providing a solid scientific foundation for the development of innovative, potent bioactive peptide products, the review aims to further research and interest in using bioactive peptides.
... In people with hypertension, the presence of ACE inhibitors is crucial to lowering angiotensin II levels and increasing bradykinin, resulting in vasodilation and reduced blood pressure. To date, seaweed species Acrochaetium sp. and Gracilariopsis lemaneiformis have been reported to possess antihypertensive activity (Deng et al., 2018;Windarto et al., 2022). ...
Pyropia vietnamensis is one of the most abundant seaweeds in the Indo-Pacific region. This study aimed to perform an in silico evaluation of P. vietnamensis proteins as potential precursors of bioactive peptides and to determine the novel peptide in terms of its half maximal inhibitory concentration (IC50) and the stability under controlled laboratory environment (in vitro) towards the dominant biological activity. The proteomic profiles of P. vietnamensis proteins were determined using LC-MS/MS analysis. Next, five proteins were chosen and employed for in silico analysis using the BIOPEP-UWM database. The in vitro characterizations of novel peptide were carried out using a dipeptidyl peptidase-IV (DPP-IV) inhibitor screening assay kit. In silico analysis revealed that DPP-IV and angiotensin-converting enzyme (ACE) inhibitors were the most potential bioactive peptides in P. vietnamensis proteins. Calpain 2, papain, pepsin (pH>2), and stem bromelain were predicted as the enzymes with the most potential to produce DPP-IV and ACE inhibitors. The novel peptides predicted were CFA, ACF, RFPS, DEWG, NYCL, CVPR, and DACF. The synthesized CVPR with an IC50 of 0.66 mg/ml exhibited stability at pH 3-7, 30-50 °C, and resisted gastrointestinal digestion. This study revealed P. vietnamensis proteins could offer health benefits due to the therapeutic potential with sustainable industrial applications on functional foods, nutraceuticals, and pharmaceuticals.
... The protein hydrolysate was isolated by chromatography, and VGGSDLQAL (VL-9) was identified. The peptide VL-9 shows the ACE inhibitory activity with IC50 value 433.1 ± 1.08 µM [94]. Duan et al. [95] isolated and characterized the novel ACE inhibitory peptides FQW, FRW, and CPF from rapeseed. ...
Background/Objectives: At present, a large number of bioactive peptides have been found from plant sources with potential applications for the prevention of chronic diseases. By promoting plant-derived bioactive peptides (PDBPs), we can reduce dependence on animals, reduce greenhouse gas emissions, and protect the ecological environment. Methods: In this review, we summarize recent advances in sustainably sourced PDBPs in terms of preparation methods, biological activity, structure–activity relationships, and their use in chronic diseases. Results: Firstly, the current preparation methods of PDBPs were summarized, and the advantages and disadvantages of enzymatic method and microbial fermentation method were introduced. Secondly, the biological activities of PDBPs that have been explored are summarized, including antioxidant, antibacterial, anticancer and antihypertensive activities. Finally, based on the biological activity, the structure–activity relationship of PDBPs and its application in chronic diseases were discussed. All these provide the foundation for the development of PDBPs. However, the study of PDBPs still has some limitations. Conclusions: Overall, PDBPs is a good candidate for the prevention and treatment of chronic diseases in humans. This work provides important information for exploring the source of PDBPs, optimizing its biological activity, and accurately designing functional foods or drugs.
... Villaró, Jiménez-Márquez, Musari, Bermejo, and Lafarga (2023) also showed that papain and ficin were anticipated to be the superior enzymes in releasing high quantities of antioxidant, renin inhibitory, DPP-IV inhibitory, and ACE inhibitory peptides from A. platensis. To understand the inhibitory mechanisms of bioactive peptides, in silico molecular docking simulation can be employed to predict the possible binding orientation of bioactive peptides onto the enzyme active sites via interaction and binding energies Windarto, Lee, Nursyam, & Hsu, 2022). In general, the higher negativity of binding free energy value means the greater binding affinity and stability between the enzyme and docked peptides were predicted, indicating more potent inhibiting effects (Li et al., 2021). ...
... Inspired by the discovery of the first ACE inhibitor drug (Captopril) derived from a snake venom peptide [12] and the commercialization of functional foods containing ACE inhibitory peptides (Ameal S™, Calpis Co., Ltd., Japan and Evolus™, Valio Ltd., Finland) [13], the exploration of ACE inhibitory (ACEI) peptides derived from natural proteins has ascended significantly. e.g., ACEI peptides derived from red algae (Acrochaetium sp.) [14], milk [15], Thai jasmine rice bran [16], scorpion venom [17], insects [18], plants [19], and animal products [20] have recently been explored. Nevertheless, the screening method to efficiently screen ACE inhibitory peptides originating from natural proteins is also crucial. ...
Taiwan red quinoa (Chenopodium formosanum Koidz.) is a pseudo-cereal crop native to Taiwan with a rich protein content that can potentially be a bioactive peptide precursor, such as angiotensin-I converting enzyme inhibitory (ACEI) peptides. Taiwan red quinoa seed protein (TRQSP) thermolysin hydrolysate showed a relatively potent ACE IC50 value of 58.5 µg/mL. After two sequential bioassay-guided fractionations, fraction F4.3 showed the best ACEI activity (89.3%). Liquid chromatography-tandem high-resolution mass spectrometry (LC-HRMS) incorporated with de novo peptide sequencing and database searching were performed to identify the peptide sequences from fraction F4.3. Based on the in silico study, three potential ACEI peptides (LGAVPPRY, IARDSAAVF, and VYLAELHF) were synthesized to identify their ACEI activity. The ACE IC50 values of LGAVPPRY (LY8), IARDSAAVF (IF9), and VYLAELHF (VF8) were calculated as 29.3, 56.4, and 115.7 µM, respectively. LY8 was a non-competitive inhibitor, while IF9 and VF8 were competitive ACE inhibitors, as confirmed by the inhibition mechanism and simulation of molecular docking studies. The ACEI pre-incubation assay suggested that LY8 was a true inhibitor type; in the meantime, IF9 and VF8 were pro-drug inhibitor types. To our best knowledge, this is the first study to screen ACEI thermolytic peptides derived from Taiwan red quinoa seed protein.
... Many potent bioactive peptides have been purified from these hydrolysates. Particularly, new ACE inhibitory peptides were purified from algae WSP hydrolyzed by thermolysin [9], and inhibition mechanism was found competitive and non-competitive [9,10]. Recently, the analysis of the whole chloroplast genome from dulse was used as a tool for a wide characterization of bioactive peptides in the sequence of chloroplast proteins [3]. ...
... Many potent bioactive peptides have been purified from these hydrolysates. Particularly, new ACE inhibitory peptides were purified from algae WSP hydrolyzed by thermolysin [9], and inhibition mechanism was found competitive and non-competitive [9,10]. Recently, the analysis of the whole chloroplast genome from dulse was used as a tool for a wide characterization of bioactive peptides in the sequence of chloroplast proteins [3]. ...
In this study, we studied the bioactive peptides produced by thermolysin hydrolysis of a water-soluble protein (WSP) from the red alga Gracilariopsis chorda, whose major components are phycobiliproteins and Ribulose-1,5-bisphosphate carboxylase-oxygenase (RuBisCo). The results showed that WSP hydrolysate exhibited significantly higher ACE inhibitory activity (92% inhibition) compared to DPP-IV inhibitory activity and DPPH scavenging activity. The phycobiliproteins and RuBisCo of G. chorda contain a high proportion of hydrophobic (31.0–46.5%) and aromatic (5.1–46.5%) amino acid residues, which was considered suitable for the formation of peptides with strong ACE inhibitory activity. Therefore, we searched for peptides with strong ACE inhibitory activity and identified two novel peptides (IDHY and LVVER). Then, their interaction with human ACE was evaluated by molecular docking, and IDHY was found to be a promising inhibitor. In silico analysis was then performed on the structural factors affecting ACE inhibitory peptide release, using the predicted 3D structures of phycobiliproteins and RuBisCo. The results showed that most of the ACE inhibitory peptides are located in the highly solvent accessible α-helix. Therefore, it was suggested that G. chorda is a good source of bioactive peptides, especially ACE-inhibitory peptides.
To reveal potent ACE inhibitors, researchers screen various bioactive peptides from several sources, and more attention has been given to aquatic sources. This review summarizes the recent research achievements on marine peptides with ACE-inhibitory action and application. Marine peptides are considered excellent bioactives due to their large structural diversity and unusual bioactivities. The mechanisms by which these marine peptides inhibit ACE include competitive binding to ACEs’ active site, interfering with ACE conformational changes, and avoiding the identification of substrates. The unique 3D attributes of marine peptides confer inhibition advantages toward ACE activity. Because IC50 values of marine peptides’ interaction with ACE are low, structure-based research assumes that the interaction between ACE and peptides increased the therapeutic application. Numerous studies on marine peptides focused on the sustainable extraction of ACE-inhibitory peptides produced from several fish, mollusks, algae, and sponges. Meanwhile, their potential applications and medical benefits are worth investigating and considering. Due to these peptides exhibiting antioxidant, antihypertensive, and even antimicrobial properties simultaneously, their therapeutic potential for cardiovascular disease and other illnesses only increases. In addition, as marine peptides show better pharmacological benefits, they have increased absorption rates and low toxicity and could perhaps be modified for better stability and bioefficacy. Biotechnological advances in peptide synthesis and formulation have greatly facilitated the generation of peptide-based ACE inhibitors from marine sources, which subsequently offer new treatment models. This article gives a complete assessment of the present state of knowledge about marine organism peptides as ACE inhibitors. In addition, it emphasizes the relevance of additional investigation into their mechanisms of action, the optimization of manufacturing processes, and assessment in in vivo, preclinical, and clinical settings, underlining the urgency and value of this study. Using marine peptides for ACE inhibition not only broadens the repertory of bioactive compounds but also shows promise for tackling the global health burden caused by cardiovascular diseases.
