Journal of Peptide Science最新文献_第2页

Regulatory Guidelines for the Analysis of Therapeutic Peptides and Proteins

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2025-02-08 DOI: 10.1002/psc.70001

Yomnah Y. Elsayed, Toni Kühl, Diana Imhof

{"title":"Regulatory Guidelines for the Analysis of Therapeutic Peptides and Proteins","authors":"Yomnah Y. Elsayed, Toni Kühl, Diana Imhof","doi":"10.1002/psc.70001","DOIUrl":"https://doi.org/10.1002/psc.70001","url":null,"abstract":"<p>Peptides and proteins have become increasingly important in the treatment of various diseases, including infections, metabolic disorders, and cancers. Over the past decades, the number of approved peptide- and protein-based drugs has grown significantly, now accounting for about 25% of the global pharmaceutical market. This increase has been recorded since the introduction of the first therapeutic peptide, insulin, in 1921. Therapeutic peptides and proteins offer several advantages over small molecule drugs, including high specificity, potency, and safety; however, they also face challenges related to instability in liquid formulations. To address this issue, numerous formulation techniques have been developed to enhance their stability. In either state, physical and chemical characterization of the peptide or protein of interest is crucial for ensuring the identity, purity, and activity of these therapeutic agents. Regulatory bodies such as the FDA, ICH, and EMA have established guidelines for the analysis, stability testing, and quality control of peptides and biologics to ensure the safety and effectiveness of these drugs. In the present review, these guidelines and the consequences thereof are summarized and provided to support the notion of developing tailored bioanalytical workflows for each peptide or protein drug.</p>","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 3","pages":""},"PeriodicalIF":1.8,"publicationDate":"2025-02-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/psc.70001","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143362643","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Synthesis of Anabaenopeptins With a Strategic Eye Toward N-Terminal Sequence Diversity

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2025-02-06 DOI: 10.1002/psc.70003

Naresh M. Venneti, Boddu S. Ramakrishna, Zoee K. Harris, Sydney C. Kasmer, Dennis P. Anderson, Nicholas J. Peraino, Judy A. Westrick, Jennifer L. Stockdill

引用次数: 0

Assessment of Phage-Displayed Peptides Targeting Cancer Cell Surface Proteins: A Comprehensive Molecular Docking Study

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2025-02-04 DOI: 10.1002/psc.70004

Verónica Quilumba-Dutan, Clara Carreón-Álvarez, Víctor Sanabria-Ayala, Sergio Hidalgo-Figueroa, Swaroop Chakraborty, Eugenia Valsami-Jones, Rubén López-Revilla, José Luis Rodríguez-López

{"title":"Assessment of Phage-Displayed Peptides Targeting Cancer Cell Surface Proteins: A Comprehensive Molecular Docking Study","authors":"Verónica Quilumba-Dutan, Clara Carreón-Álvarez, Víctor Sanabria-Ayala, Sergio Hidalgo-Figueroa, Swaroop Chakraborty, Eugenia Valsami-Jones, Rubén López-Revilla, José Luis Rodríguez-López","doi":"10.1002/psc.70004","DOIUrl":"https://doi.org/10.1002/psc.70004","url":null,"abstract":"<div>\u0000 \u0000 <p>Peptides binding overexpressed breast and cervical cancer cell surface proteins can be isolated by phage display technology, and their affinity to their potential receptors can be assessed by molecular docking. We isolated 44 phage clones displaying dodecapeptides with high affinity to HeLa cervical cancer and MDA-MB-231 (MDA) breast cancer cells by repeated biopanning of an MK13 phage library and explored their affinity to specific proteins by molecular docking. Six peptides appeared repeatedly during biopanning: two with affinity to HeLa (H5/H21), and four with affinity to MDA cells (M3/M7/M15/M17). Peptide pairs M3/H5 and H1/M17 had affinity to both cell lines. A systematic review identified Annexin A2, EGFR, CD44, CD146, and Integrin alpha V as potential protein targets in HeLa cells, and Vimentin, Galectin-1, and Annexins A1 and A5 in MDA cells. Via virtual screening, we selected six peptides with the highest total docking scores: H1 (−916.32), H6 (−979.21), H19 (−1093.24), M6 (−732.21), M16 (−745.5), and M19 (−739.64), and identified that docking scores were strengthened by the protein type, the interacting amino acid side chains, and the polarity of peptides. This approach facilitates the selection of relevant peptides that could be further explored for active targeting in cancer diagnosis and treatment.</p>\u0000 </div>","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 3","pages":""},"PeriodicalIF":1.8,"publicationDate":"2025-02-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143111721","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Self-Assembly of a Conjugate of Lipoic Acid With a Collagen-Stimulating Pentapeptide Showing Cytocompatibility and Wound Healing Properties, and Chemical and Photolytic Disassembly

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2025-02-04 DOI: 10.1002/psc.70002

Lucas R. de Mello, Valeria Castelletto, Leide Cavalcanti, Jani Seitsonen, Ian W. Hamley

{"title":"Self-Assembly of a Conjugate of Lipoic Acid With a Collagen-Stimulating Pentapeptide Showing Cytocompatibility and Wound Healing Properties, and Chemical and Photolytic Disassembly","authors":"Lucas R. de Mello, Valeria Castelletto, Leide Cavalcanti, Jani Seitsonen, Ian W. Hamley","doi":"10.1002/psc.70002","DOIUrl":"https://doi.org/10.1002/psc.70002","url":null,"abstract":"<p>Lipoic acid is a biocompatible compound with antioxidant activity that is of considerable interest in cosmetic formulations, and the disulfide group in the N-terminal ring confers redox activity. Here, we study the self-assembly and aspects of the bioactivity of a lipopeptide (peptide amphiphile) comprising the KTTKS collagen-stimulating pentapeptide sequence conjugated to an N-terminal lipoic acid chain, lipoyl-KTTKS. Using SAXS, SANS and cryo-TEM, lipoyl-KTTKS is found to form a population of curly fibrils (wormlike micelles) above a critical aggregation concentration. Upon chemical reduction, the fibrils (and β-sheet structure) are disrupted because of the breaking of the disulfide bond, which produces dihydrolipoic acid. Lipoyl-KTTKS also undergoes photo-degradation in the presence of UV radiation. Through cell assays using fibroblasts, we found that lipoyl-KTTKS has excellent cytocompatibility across a wide concentration range, stimulates collagen production, and enhances the rate of cell coverage in a simple in vitro scratch assay of ‘wound healing’. Lipoyl-KTTKS thus has several notable properties that may be useful for the development of cosmetics, cell scaffolds or tissue engineering materials.</p>","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 3","pages":""},"PeriodicalIF":1.8,"publicationDate":"2025-02-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/psc.70002","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143111722","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

The Prototypical Oligopeptide Transporter YdgR From E. coli Exhibits a Strict Preference for β-Ala-Lys(AMCA) 大肠杆菌原型低聚肽转运体 YdgR 对 β-Ala-Lys(AMCA)具有严格的偏好。

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2025-01-26 DOI: 10.1002/psc.3670

Salvia Sajid, Cecilia Ninh, Ruyu Yan, Maria Rafiq, Lars Porskjær Christensen, Mikkel Girke Jørgensen, Paul Robert Hansen, Henrik Franzyk, Osman Mirza, Bala Krishna Prabhala

{"title":"The Prototypical Oligopeptide Transporter YdgR From E. coli Exhibits a Strict Preference for β-Ala-Lys(AMCA)","authors":"Salvia Sajid, Cecilia Ninh, Ruyu Yan, Maria Rafiq, Lars Porskjær Christensen, Mikkel Girke Jørgensen, Paul Robert Hansen, Henrik Franzyk, Osman Mirza, Bala Krishna Prabhala","doi":"10.1002/psc.3670","DOIUrl":"10.1002/psc.3670","url":null,"abstract":"<div>\u0000 \u0000 <p>Fluorescent probes are widely used in cellular imaging and disease diagnosis. Acting as substitute carriers, fluorescent probes can also be used to help transport drugs within cells. In this study, commonly used fluorophores, TAMRA (5-carboxytetramethylrhodamine), PBA (1-pyrenebutyric acid), NBD (nitrobenzoxadiazole), OG (Oregon Green), and CF (5-carboxyfluorescein) were conjugated with the dipeptide β-Ala-Lys, the peptide moiety of the well-established peptide transporter substrate β-Ala-Lys(AMCA) (AMCA: 7-amino-4-methyl-coumarin-3-acetic acid) by modifying it with respect to side-chain length and functional end groups. The analogs were tested for transport through or inhibition of YdgR, a prototypical peptide transporter from <i>E. coli</i> and apparently homologous to the human PEPT1. Strikingly, none of the dipeptide-fluorophore conjugates nor minor modifications in the reporter substrate were tolerated by YdgR, indicating discrepancies to PEPT1. These findings underscore intricate substrate recognition mechanisms governing substrate recognition by YdgR.</p>\u0000 </div>","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 3","pages":""},"PeriodicalIF":1.8,"publicationDate":"2025-01-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143047075","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Investigation of the Potency of KALA and REV Cell-Penetrating Peptides for In Vitro/In Vivo Delivery of an HPV Multiepitope DNA Construct

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2025-01-23 DOI: 10.1002/psc.70000

Haleh Feyzyab, Alireza Milani, Elnaz Agi, Mehrdad Hashemi, Azam Bolhassani

{"title":"Investigation of the Potency of KALA and REV Cell-Penetrating Peptides for In Vitro/In Vivo Delivery of an HPV Multiepitope DNA Construct","authors":"Haleh Feyzyab, Alireza Milani, Elnaz Agi, Mehrdad Hashemi, Azam Bolhassani","doi":"10.1002/psc.70000","DOIUrl":"10.1002/psc.70000","url":null,"abstract":"<div>\u0000 \u0000 <p>Developing human papillomavirus (HPV) therapeutic DNA vaccines requires an effective delivery system, such as cell-penetrating peptides (CPPs). In the current study, the multiepitope DNA constructs harboring the immunogenic and conserved epitopes of the L1, L2, and E7 proteins of HPV16/18 (pcDNA-L1-L2-E7 and pEGFP-L1-L2-E7) were delivered using KALA and REV CPPs with different properties in vitro and in vivo. Herein, after confirmation of the REV/DNA and KALA/DNA complexes, their stability was investigated against DNase I and serum protease. Then, their entry into HEK-293T eukaryotic cells was analyzed by qualitative and quantitative methods. Finally, anti-tumor effects of the peptide/DNA complexes were investigated in the C57BL/6 mouse model. Based on the obtained data, the REV/DNA and KALA/DNA complexes at the N/P ratio of 5:1 demonstrated successful penetration into HEK-293T cells. Furthermore, in vivo studies represented that the REV/DNA (survival rate: 75%) and KALA/DNA (survival rate: 50%) complexes provided significant protection against C3 tumors in mice. Indeed, REV CPP exhibited a higher survival rate and lower tumor volume than KALA CPP, 50 days after the C3 challenge. These findings represented the potential of KALA and REV CPPs, especially REV, as promising gene delivery systems for developing HPV therapeutic DNA vaccine candidates.</p>\u0000 </div>","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 3","pages":""},"PeriodicalIF":1.8,"publicationDate":"2025-01-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143033374","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

A Novel Insect Short Neuropeptide sNPF Peptidomimetic Insecticide: Rational Design, Synthesis, and Aphicidal Activity Study 一种新型昆虫短神经肽sNPF类肽类杀虫剂：合理设计、合成及杀虫活性研究。

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2025-01-20 DOI: 10.1002/psc.3669

Yuanlin Zhou, Chunyue Wang, Tong Lin, Qingdong Ji, Qin Han, Anzhi Liu, Jiajia Chen, Tong Liu, Wenyi Ran

{"title":"A Novel Insect Short Neuropeptide sNPF Peptidomimetic Insecticide: Rational Design, Synthesis, and Aphicidal Activity Study","authors":"Yuanlin Zhou, Chunyue Wang, Tong Lin, Qingdong Ji, Qin Han, Anzhi Liu, Jiajia Chen, Tong Liu, Wenyi Ran","doi":"10.1002/psc.3669","DOIUrl":"10.1002/psc.3669","url":null,"abstract":"<div>\u0000 \u0000 <p>Short neuropeptide F (sNPF) is an insect-specific neuropeptide named for its C-terminal phenylalanine. It consists of 6–19 amino acids with a conserved RLRFa structure, regulating feeding, growth, circadian rhythms, and water-salt balance in insects. Its receptor belongs to GPCR-As and binds sNPF to regulate the insect nervous system. Many research groups are evaluating sNPF for plant protection and pest control. In this study, the natural sNPF from the pea aphid (<i>Acyrthosiphon pisum</i>) was used as a lead compound. Five novel sNPF analogs were designed and synthesized through molecular docking and peptidomimetics, altering the N-terminal amino acid to Ser, Thr, Tyr, Leu, or Gln. Aphid bioassays showed that the analog I-3 (YLRLRFa, LC<sub>50</sub> = 1.820 mg/L) was more active than the natural Acypi-sNPF-1 and pymetrozine. The structure–activity relationship analysis indicated that N-terminal tyrosine incorporation, combined with increased Clog<i>P</i> and TPSA, enhanced aphidicidal activity. Furthermore, Toxtree's toxicity predictions suggest a low risk for all compounds, and a toxicity assay conducted on the honeybee (<i>Apis mellifera</i>) for I-3, which exhibits high aphidicidal activity, indicates that I-3 does not pose a toxicity risk to non-target organisms. Thus, I-3 can be utilized as a selective and environmentally friendly insecticide to manage pea aphids.</p>\u0000 </div>","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 3","pages":""},"PeriodicalIF":1.8,"publicationDate":"2025-01-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143007231","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Overview of Peptides and Their Potential Roles in Skin Health and Beauty 多肽综述及其在皮肤健康和美容中的潜在作用。

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2025-01-07 DOI: 10.1002/psc.3668

Leyang Wang, Zhijing Wu, Xinyu Wang, Xiaoli Wang, Jingzhuo Mao, Yan Yan, Lu Zhang, Zhuzhen Zhang

{"title":"Overview of Peptides and Their Potential Roles in Skin Health and Beauty","authors":"Leyang Wang, Zhijing Wu, Xinyu Wang, Xiaoli Wang, Jingzhuo Mao, Yan Yan, Lu Zhang, Zhuzhen Zhang","doi":"10.1002/psc.3668","DOIUrl":"10.1002/psc.3668","url":null,"abstract":"<div>\u0000 \u0000 <p>Peptides are molecules that consist of at least two amino acids linked by peptide bonds. The difference between peptides and proteins is primarily based on size and structure. Typically, oligopeptides consist of fewer than about 10–20 amino acids, and polypeptides consist of more than 20 amino acids, whereas proteins usually are made up more than 50 amino acids and often contain multiple peptide subunits as stated in the International Union of Pure and Applied Chemistry rules. Beyond the nutritional properties, peptides are also structural components of hormones, enzymes, toxins, and antibiotics and play several fundamental physiological roles in the body. Since the introduction of the first commercial peptide drug, insulin, peptide-based drugs have gained increased interest. So far, more than 80 peptide-based drugs have reached the market for a wide range of conditions, such as diabetes, cardiovascular diseases, and urological disorders. Meanwhile, peptides have also gained significant attention in the cosmetic industry because of their potential in boosting skin health. In this review, peptides were comprehensively summarized in the aspects of sources, function, the use of peptides in cosmetics and skin care, and indications for the delivery of cosmetic peptides.</p>\u0000 </div>","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 2","pages":""},"PeriodicalIF":1.8,"publicationDate":"2025-01-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142950523","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

PepFuNN: Novo Nordisk Open-Source Toolkit to Enable Peptide in Silico Analysis PepFuNN：诺和诺德开源工具包，使肽在硅分析。

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2025-01-07 DOI: 10.1002/psc.3666

Rodrigo Ochoa, Kristine Deibler

引用次数: 0

Crystallographic Analysis of Short Helical Peptides Containing Homologs of Phenylalanine 含有苯丙氨酸同源物的短螺旋肽的晶体学分析。

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2024-12-30 DOI: 10.1002/psc.3667

Mrinal Kalita, Archana, Ramesh Ramapanicker, Prema G. Vasudev

{"title":"Crystallographic Analysis of Short Helical Peptides Containing Homologs of Phenylalanine","authors":"Mrinal Kalita,  Archana, Ramesh Ramapanicker, Prema G. Vasudev","doi":"10.1002/psc.3667","DOIUrl":"10.1002/psc.3667","url":null,"abstract":"<div>\u0000 \u0000 <p>Interactions between aromatic side chains of amino acids stabilize the fold and assembly of short peptides. The aromatic π…π and C-H…π interactions have been widely explored in the design of short peptides with specific folding and aggregation patterns. In the present study, we investigated the effect of homologated phenylalanine side chains on the conformation and assembly of peptide helices through X-ray crystallographic structure determination and analysis of five pentapeptides. The parent peptide Boc-Phe-Aib-Aib-Leu-Phe-NHiPr (<b>1</b>) and its four variations were synthesized, in which either one or both of the Phe side chains have been modified by inserting one (homophenylalanine, hPhe; -CH<sub>2</sub>-CH<sub>2</sub>-C<sub>6</sub>H<sub>5</sub>) or two (h<sup>2</sup>Phe; -CH<sub>2</sub>-CH<sub>2</sub>-CH<sub>2</sub>-C<sub>6</sub>H<sub>5</sub>) additional CH<sub>2</sub> groups in the side chain, and their crystal structures were analyzed. The results show that intramolecular aromatic interactions are not present in the parent peptide but are present in the peptides containing the higher homologs of Phe. In peptides that did not show intramolecular aromatic interactions, the effect of increased length of the side chain of Phe residues manifested as intermolecular interactions leading to ordered packing in crystals. The results indicate the potential of hPhe and h<sup>2</sup>Phe residues to have aromatic interactions that could induce preferential folding and aggregation of peptides containing them.</p>\u0000 </div>","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 2","pages":""},"PeriodicalIF":1.8,"publicationDate":"2024-12-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142907208","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0