Protein and Peptide Letters (PROTEIN PEPTIDE LETT )

Publisher: Bentham Science Publishers

Description

Protein and Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merits rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function. Protein and Peptide Letters will focus on: Structure Studies, Recombinant Expression, Drug Design, Chemical Synthesis, Function, Pharmacology, Enzymology, Immunology, Biotechnology, Protein Engineering, Protein Folding, Sequencing, Molecular Recognition, Purification and Analysis.

  • Impact factor
    1.99
    Show impact factor history
     
    Impact factor
  • 5-year impact
    1.71
  • Cited half-life
    3.60
  • Immediacy index
    0.49
  • Eigenfactor
    0.01
  • Article influence
    0.35
  • Website
    Protein and Peptide Letters website
  • Other titles
    Protein and peptide letters (Online)
  • ISSN
    0929-8665
  • OCLC
    60638050
  • Material type
    Document, Periodical, Internet resource
  • Document type
    Internet Resource, Computer File, Journal / Magazine / Newspaper

Publisher details

Bentham Science Publishers

  • Pre-print
    • Author can archive a pre-print version
  • Post-print
    • Author cannot archive a post-print version
  • Restrictions
    • 12 months (unless federal, government, funding agencies or local policy mandates for the author's institute a different policy on self-archiving)
  • Conditions
    • On authors personal or authors institutions server
    • Published source must be acknowledged
    • Must link to journal home page
    • Publisher's version/PDF cannot be used
    • Articles in all journals can be made Open Access on payment of additional charge
  • Classification
    ​ yellow

Publications in this journal

  • [Show abstract] [Hide abstract]
    ABSTRACT: The pH stability of lectin from black turtle bean was characterized by a variety of biophysical techniques over the pH range from 2.0 to 10.0. The zero-order and second-derivative UV spectra at different pH values indicated that the tertiary structure of the protein does not change significantly with changes in pH. The maxima emission fluorescence of the lectin upon excitation at 280 nm and 295 nm were found to be blue shifted 1.2 nm at pH 2.0, and with a red-shift of 1.0 nm at pH 10.0. The chemical denaturation results obtained by monitoring the intrinsic fluorescence of the lectin indicated that unfolding of the protein induced by guanidine hydrochloride (GdnHCl) could be described using a three-state model. Complete unfolding of the protein was observed at pH 7.2 in the presence of 6.5 M GdnHCl after 2 weeks, which suggested that the lectin was stable at various pHs. Irreversible thermal denaturation of lectin was also investigated at various pHs by differential scanning calorimetry (DSC). The first-order two-state kinetic model was applied to explain the scan-rate dependent DSC transitions. Both the higher activation energy (Ea) computed from the irreversible thermal denaturation and the three-state chemical denaturation process suggested that the lectin structure remained significantly unchanged from pH 2.0 to 10.0, which indicated that the structure of the lectin was stable over a wide pH range.
    Protein and Peptide Letters 09/2014;
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    ABSTRACT: An inducible and aromatic nitrilase from Gordonia terrae was purified with a yield of 19%. The enzyme had turnover number of 63 s-1x 10-3, Km 1.4 mM and Vmax 95 Umg-1 protein for benzonitrile. The nitrilase of G. terrae was active at basic pH (7-10), moderate temperature (20-45 ºC) and has a half-life of 4 h at 35 ºC. MALDI analysis and amino acid sequence deduced from cloned nucleotide fragment showed 97% homology with putative amidohydrolase of Gordonia sputi NBRC 100414 and G. namibiensis. The enzyme showed regio-selectivity towards hydroxybenzonitriles, as different position of hydroxyl group i.e. meta-, para- and ortho- substitutions on benzonitrile effect enzyme activity. The in-silico interactions of these substrates with the predicted 3D model of this enzyme also showed differential interaction between hydroxyl group of substrates and the polar amino acids surrounding enzyme's active site. This leads to different proximity and orientation of substrates vis-a-vis their interaction with catalytic residues.
    Protein and Peptide Letters 09/2014;
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    ABSTRACT: Firefly luciferase is a relatively unstable protein and commonly loses its activity at room temperature because of structural changes. The structural and functional stability of this protein is critical for its enzymatic applications. Different approaches are applied to increase the stability of this enzyme such as designing of covalent cross-links (disulfide bonds). In this study, luciferase mutants containing one or two disulfide bonds were compared to the native protein for their structural, thermodynamic, and functional properties. Mutant forms of P. Pyralis luciferase A296C-A326C and A296C-A326C/P451C-V469C were used. Thermodynamic and biophysical studies were carried out using UV-Vis, fluorescence, circular dichroism, luminescence spectroscopy and differential scanning calorimetry (DSC). We observed that both mutant forms of the protein were more stable than the wild-type enzyme. However, the single disulfide bond containing mutant was structurally and functionally more stable than the mutant protein containing two disulfide bonds. Furthermore, the enzymatic activity of the single disulfide bond containing mutant protein was 7-folds greater than the wild type and the double disulfide bond proteins. The A296C-A326C mutation also increased the reversibility and disaggregation of the protein. The enhanced activity of the single disulfide bond mutant protein was contributed to the expansion of its active site cleft, which was confirmed by bioinformatics tools.
    Protein and Peptide Letters 08/2014;
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    ABSTRACT: A method of the genomic DNA immobilization on microcrystalline cellulose was described to isolate DNA-binding proteins. At first, DNA fragments were prepared by sonication and immobilized on cellulose phase. After the immobilization, DNA duplex formation was done. Using this microcrystalline cellulose affinity chromatography, DNA-binding proteins from kumquat (Fortunella margarita Swingle) leaf samples were isolated and analyzed using LC-MS/MS analysis. LC-MS/MS analysis showed that twenty-eight kinds of protein mainly including histones, protein- synthetic proteins and other DNA-binding proteins were identified. The identification list consists with the results in previous research to isolate DNA-binding proteins. It is suggested that this techniques be readily applied to isolate DNA-binding proteins.
    Protein and Peptide Letters 08/2014;
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    ABSTRACT: Shrimp ovarian peritrophin (SOP), a major protein in jelly layer and cortical rods, plays a role in egg protection after spawning. Previous study, sequence of SOP gene from Fenneropenaeus merguiensis (Fm-SOP) was composed of domain A and domain B. The SOP domain A contains amino acid sequences between 1-80 of Fm-SOP. The domain A had six conserved cysteines which have been found in many antimicrobial peptides. The molecular weight of purified rSOP-A protein was about 9 kDa. The SOP domain B contains amino acid sequences 81-329 of Fm-SOP while SOP-B1 was amino acid sequence 182-275 of Fm-SOP. The molecular weight of purified rHis-SOP-B and rHis-SOP-B1 protein were about 38.5 and 18.0 kDa, respectively. Antimicrobial activities of rSOP-A, rHis-SOP-B and rHis-SOP-B1 protein were investigated by liquid growth inhibition assay. Minimal Inhibition Concentration (MIC) of rSOP-A against Staphylococcus aureus, Escherichia coli, Vibrio harveyi, Candida albicans and Fusarium oxysporum were 35, 280, 280, 570 and 15 µg/ml, respectively. The MIC of rHis-SOP-B against S. aureus, V. harveyi and F. oxysporum were 30, 270 and 500 µg/ml, respectively. And the MIC of rHis-SOP-B1 against S. aureus, V. harveyi and F. oxysporum were 20, 470 and 250 µg/ml, respectively. The rHis-SOP-B and rHis-SOP-B1 (1000 µg/ml) did not show antimicrobial activity against E. coli and C. albicans. Three purified proteins were able to agglutinate V. harveyi in vitro, displayed a chitinase activity and proteinase inhibition. In addition the stability of the proteins was tested and found decrease antimicrobial activity after incubation at 50 °C for 5 h.
    Protein and Peptide Letters 08/2014;
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    ABSTRACT: Secreted phospholipase A2 (sPLA2) molecules constitute a family of proteins that are involved functionally in many biological processes. In particular, they participate in diverse pathophysiological settings as enzymes that release free fatty acids and lysophospholipids from phospholipids in biological membranes, or as ligands for various cellular receptors. In this review the confirmed or expected functions of sPLA2s in the mammalian immune system are surveyed. Some of the twelve mammalian sPLA2 molecules constitute part of the so-called innate immune system by virtue of their antibacterial, antiviral and antifungal activities. They are also involved in acute inflammation, a protective reaction of the body to infection or injury. The acute inflammation sometimes escapes regulation, becomes chronic and can evolve into a severe pathology. One or more types of sPLA2 are involved in asthma, rheumatoid arthritis, sepsis, atherosclerosis, myocardial infarction, Crohn's disease, ulcerative colitis and cancer. sPLA2s are thus important therapeutic targets as well as biotherapeutic molecules. Improving the selectivity of inhibitors of sPLA2s to be able to target a particular sPLA2 could therefore be one of the most important tasks for future research.
    Protein and Peptide Letters 08/2014;
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    ABSTRACT: Proteases regulating inflammation are versatile enzymes, usually extracellular matrix degrading enzymes that are involved in wound healing, angiogenesis, coagulation, development, apoptosis and other physiological processes. Their dysregulation and increased expression during inflammation can have devastating consequences, promoting etiology of vascular diseases, inflammatory arthritis, cancer, and allograft rejection. In this review several proteases (ADAMTS, granzymes, plasmin, and kallikreins) with different mechanisms and substrates are described in addition to their physiological roles and contribution to inflammation and inflammatory diseases. Inhibition of proteases may therefore represent an attractive strategy for treatment and herein we describe physiological and engineered inhibitors.
    Protein and Peptide Letters 08/2014;
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    ABSTRACT: In the last few decades, novel drug delivery strategies have been received a big priority to the formulation scientists. Among the various methods, techniques, and systems, peptides and proteins have drawn a special attention for their wide scope in the area. Serum albumin, transferrin, recombinant proteins, virus capsids are used as carrier for drug and biomolecules. Conjugates of polymers with proteins have also shown strong potency in the field of drug delivery. Polyethylene glycol is one of the most successful polymers that has been used extensively to develop protein conjugated formulations. Besides, polyvinyl pyrrolidone, poly lactic-co-glycolic acid, N-(2-hydroxypropyl) methacrylamide copolymer, polyglutamic acid have also been investigated. In this review, we will highlight on the most recent overview of various advantages, limitations and marketed products of proteins, peptides and protein/peptide-polymer conjugates as drug carriers, such products in clinical trials and their various uses in the field of modern drug delivery. Understanding the key features of these materials and the vigorous research in this field will develop new drug formulations that will combat various types of life-threatening diseases.
    Protein and Peptide Letters 08/2014;
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    ABSTRACT: α-Amylases hydrolyze α- 1,4-glycosidic bonds during assimilation of biological macromolecules. The amino acid sequences of these enzymes in thousands of diverse organisms are known and the 3D structures of several proteins have been solved. The 3D structure analysis of these universal enzymes from diverse organisms has been studied by the generation of phylogenetic trees and structure based sequence analysis to generate a metric for the degree of conservation that is responsible for individual speciation. Greater similarities are observed between reference NCBI tree and structure based phylogenetic tree compared to sequence based phylogenetic tree indicating that structures truly represent the functional aspects of proteins than from the sequence information alone. We report differences in the profile specific conserved and insertion/deletion regions, factors responsible for the Ca2+ and Cl- ion binding and the disulfide connectivity pattern that discriminate the enzymes over evolution.
    Protein and Peptide Letters 07/2014; 21(9):948-956.
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    ABSTRACT: We have identified intrinsically unstructured C-terminus of a Bacillus lipase. In an effort to understand the possible role of this C-terminus unstructured region, 10, 20 and 30 amino acids were serially deleted from C-terminal region of the lipase. The catalytic properties of wild type and resulted truncated enzymes were compared. Deletion of 10 amino acids from C-terminus region resulted in decrease in transcription of lipase, specific enzyme activity and extracellular secretion of lipase in comparison to wild type while no effect on lipase aggregation. Negligible activity was observed upon deletion of 20 amino acids. The homology model of the protein demonstrated that the tertiary structure of the protein was held together by these C-terminus residues due to six critically placed hydrogen bonds. Therefore C-terminus was essential for the tertiary structure and enzyme activity of lipase. Due to structural flexibility and plasticity originating from the lack of a definite-ordered 3D structure, such disordered regions might represent a major functional advantage for proteinsWe have identified intrinsically unstructured C-terminus of a Bacillus lipase. In an effort to understand the possible role of this C-terminus unstructured region, 10, 20 and 30 amino acids were serially deleted from C-terminal region of the lipase. The catalytic properties of wild type and resulted truncated enzymes were compared. Deletion of 10 amino acids from C-terminus region resulted in decrease in transcription of lipase, specific enzyme activity and extracellular secretion of lipase in comparison to wild type while no effect on lipase aggregation. Negligible activity was observed upon deletion of 20 amino acids. The homology model of the protein demonstrated that the tertiary structure of the protein was held together by these C-terminus residues due to six critically placed hydrogen bonds. Therefore C-terminus was essential for the tertiary structure and enzyme activity of lipase. Due to structural flexibility and plasticity originating from the lack of a definite-ordered 3D structure, such disordered regions might represent a major functional advantage for proteins.
    Protein and Peptide Letters 07/2014;
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    ABSTRACT: Glycopeptides with potent antibiotic activity are vital for the treatment of severe infections that are caused by gram-positive bacteria, especially methicillin-resistant Staphylococcus aureus. Recently, the glycopeptide-resistant gram-positive bacteria present a serious challenge to public health after several decades of clinical use. Additionally, the antibacterial activity and side effects are become an increasing crisis and should have to be taken into account. As a consequence, new glycopeptide antibiotics are needed to deal with these problems. In past years, with the development of natural product chemistry, more and more glycopeptide compounds with promising biological properties were discovered. In addition, the chemical modification of the known glycopeptide provides an opportunity for the discovery of new potential glycopeptide antibiotics. Considerable efforts have been made in this field in order to meet the clinical needs. In this article, we mainly focus on the advances of glycopeptide as antibiotics, including many representative glycopeptides or their analogues and derivatives. Taken together, we hope all this information is helpful for the discovery of new potential glycopeptide antibiotics.
    Protein and Peptide Letters 06/2014;
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    ABSTRACT: Peptide-N4-(N-acetyl-â-glucosaminyl) asparagine amidases (commonly known as PNGases) have been described in a wide variety of prokaryotic hosts and exist as an integral part of the lysosomal refolding machinery in all higher organisms. Since the discovery of this ubiquitous biological function of PNGases 15 years ago, research on PNGases has found growing attention within and outside of the glycobiology research community, with currently more than 30 eukaryotic and bacterial PNGases identified and well studied. Based on the research results of their structures, enzyme properties and functions, PNGases can be primarily divided into three different types: PNGase F-like, acidic PNGases, and cytoplasmic PNGases. In this review, a brief summary of the current knowledge of these three types of PNGases in respect of their general properties and applications of the commercially available PNGases in glycopeptide and glycoprotein analysis will be presented.
    Protein and Peptide Letters 06/2014;
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    ABSTRACT: The asialoglycoprotein receptor (ASGPR) is a high-capacity C-type lectin receptor expressed on mammalian hepatocytes. The main physiological function of ASGPR has not been completely clarified and is thought to be specific binding and internalization of galactose (Gal)/N-acetylgalactosamine (GalNAc)-terminating glycoproteins by hepatic parenchymal cells. The human ASGPR is comprised of two homologous polypeptides, H1 and H2. ASGPR H1 has two splice variants (H1a and H1b) and ASGPR H2 has three splice variants (H2a, H2b, and H2c). These variants have been discovered to exist both in human liver tissues and in human hepatoma cells. Variant H1b, which has an in-frame deletion of exon 2 resulting in the loss of the transmembrane domain and is secreted as a soluble protein, encodes functional soluble ASGPR (s-ASGPR). Based on our results of in vitro binding assay, we proposed the possible physiological function of s-ASGPR, which is well interpreted in the Galactosyl Homeostasis Hypothesis proposed by Weigel. ASGPR is one of the most promising targets for hepatic delivery. In this review, the recent progresses of cationic polysomes and liposomes as effective non-viral delivery system via ASGPR are also presented.
    Protein and Peptide Letters 06/2014;
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    ABSTRACT: Misfolded protein amyloid-beta protein (Aβ) and tau protein are two high hallmarks of Alzheimer's disease (AD), representing significant targets in treating AD. Research on mechanisms of the two proteins inducing neuron dysfunctions provide therapeutic strategies of AD, including inhibition of Aβ production and aggregation, acceleration of Aβ clearance as well as reduction of tau hyperphosphorylation. Proteoglycans (PGs) consist of a core protein and glycosaminoglycans (GAGs) chains, with enormous structural diversity due to variation in the core protein, the number of GAG chains as well as extent and position of sulfation. Considerable evidence has indicated that PGs and GAGs play important roles in Aβ and tau processing. Numbers of GAGs and analogues have potential therapeutic function in AD. In this Review, we focus on the relationship of PGs and GAGs with misfolded proteins in AD and their potential therapeutic implications.
    Protein and Peptide Letters 06/2014;
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    ABSTRACT: A novel and convenient strategy for iodine labeled glycopeptide molecular probe and purification was developed. The fluorine rich bi-functional coupling agent, 4-tris(2-perfluorohexylethyl)stannylbenzoate succinimidyl ester, was successfully synthesized via 5 steps starting from the fluorous Grignard reagent. It was purified by a simple and fast isolation using perfluorinated hexanes (FC-72). The "cold" iodine labeled yield for the coupling agent was as high as 92% within 15 min. The iodine-labeled product was only in organic fractions as we expected. It was shown that there was only one major peak in organic fractions according to HPLC. Finally, the iodine-labeled coupling agent was applied to label glycopeptide and afforded a high yield of 87% within 30 min.
    Protein and Peptide Letters 06/2014;
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    ABSTRACT: In 2008 cancer was identified by the World Health Organization (WHO) as one of four threats to human health and development. Since the early published reports of the first chemotherapeutic, mustine, in 1946, the anti-cancer drug and development industry has grown into a multi-billion dollar business enterprise. Worldwide, the rates of new cancer cases and deaths has been steadily increasing each year, with the estimation by the WHO-sponsored GLOBOCAN cancer database, that at current rates, nearly 13 million cancer deaths will be reported in 2030. The recent successes of monoclonal antibodies (mAbs), an important class of glycoprotein, and their multivalent and drug conjugated derivatives over the past 30 years have led to the approval of 12 monoclonal antibodies for use in cancer treatment by the FDA. Modern recombinant and engineering techniques have led to an explosion of antibody platforms that can be attributed to great gains in clinical efficacy. This review discusses and outlines a sample of mAbs currently approved for cancer treatment by the FDA, as well as antibody platforms in the research pipeline and clinic that have been engineered for greater tumor penetration, binding, and efficacy.
    Protein and Peptide Letters 06/2014;
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    ABSTRACT: Suzuki-Miyaura coupling reaction was applied in the syntheses of neoglycopeptides. This work utilizes new type of glycosyl aryl boronic acid and readily accessible iodo amino acids/iodopeptides. Both carbohydrate and peptide moieties are unprotected and the final product could be isolated directly. The neoglyco amino acid and neoglycopeptide products feature an O-glycosyl biaryl linker between the carbohydrate and peptide moieties.
    Protein and Peptide Letters 06/2014;
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    ABSTRACT: Glycoproteins are becoming increasingly relevant in therapeutics, including tissue plasminogen activator for the treatment of myocardial infarction and strokes, erythropoietin for anemia and various monoclonal antibody-based treatments for cancer. Protein N- and O-glycosylation is perhaps the most crucial and immensely complex posttranslational modification that proteins undergo, and its characterization presents a major challenge. This review will discuss current techniques for the characterization of glycoproteins, with a focus on therapeutic glycoproteins where available. The crucial analytical techniques, such as high-performance liquid chromatography (HPLC), capillary electrophoresis (CE), and mass spectrometry (MS) will be described, alongside the necessary chemical labeling methods for sensitive detection. The well-established chemical and enzymatic methods for oligosaccharide release from proteins will be discussed, as will more modern methods based on exhaustive protein hydrolysis with non-specific proteases.
    Protein and Peptide Letters 06/2014;
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    ABSTRACT: Eliciting efficient broadly neutralizing antibodies (BnAbs) is an important goal that has yet to be achieved for human immunodeficiency type 1 (HIV-1) vaccine development, although they are rarely produced in virus-infected individuals. In particular, inducing specific neutralizing antibodies to the gp41 membrane proximal external region (MPER) has proven a difficult task. In this study, we introduce Norovirus P particles as a new platform to display the MPER epitope of HIV-1 as a vaccine with the aim of enhancing immune responses. The results showed that HIV-1 chimeric P particles were capable of inducing MPER-specific antibody responses in immunized guinea pigs, although only weakly neutralizing activity could be detected. These findings are consistent with other previous studies which have also focused on the well-studied 2F5 and 4E10 BnAbs. Our findings provide an alternate strategy for design of vaccines against HIV-1. However, great challenges remain in the effort to develop vaccines that can induce efficient HIV-1 neutralizing antibodies.
    Protein and Peptide Letters 06/2014;
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    ABSTRACT: Current advancements in biological protein discovery utilize bi-partite methods of fluorescence detection where chromophore and scaffold are uncoupled. One such technology, called fluorogen-activating proteins (FAPs), consists of single-chain-variable-fragments (scFvs) selected against small organic molecules (fluorogens) that are non-fluorescent in solution, but highly fluorescent when bound to the scFv. In unusual circumstances a scFv may activate similar fluorogens from a single chemical family. In this report we identified a scFv biosensor with fluorescence activity against multiple fluorogens from two structurally dissimilar families. In-vitro analysis revealed highly selective scFv-ligand interactions at sub-micromolar ranges. Additionally, each scFv-fluorogen complex possesses unique excitation and emission spectra, which allows broader detection limits from the biosensor. Further analysis indicated that ligand activation, regardless of chemical family, occurs at a common scFv binding region that proves flexible, yet selective for fluorogen binding. As a protein reporter at the surface of mammalian cells, the scFv revealed bright signal detection and minimal background. Additionally, when tagged to a G-protein-coupled receptor, we observed agonist dependent signaling leading to protein traffic from cell surface to endosomes via multi-color fluorescence tracking. In summary, this report unveils a non-canonical scFv biosensor with properties of high ligand affinity and multi-channel fluorescence detection, which consequently offers expanded opportunities for cellular protein discovery.
    Protein and Peptide Letters 06/2014;

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