Journal of Peptide Science最新文献

Structural Modification and Antitumor Activity Study of Peptide Codesane: Discovery of Novel Stapled Peptide Antitumor Agents 肽Codesane的结构修饰及抗肿瘤活性研究：新型钉接肽抗肿瘤药物的发现

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2025-05-23 DOI: 10.1002/psc.70012

Qingmei Li, Lijuan Qiu, Yong Li

{"title":"Structural Modification and Antitumor Activity Study of Peptide Codesane: Discovery of Novel Stapled Peptide Antitumor Agents","authors":"Qingmei Li, Lijuan Qiu, Yong Li","doi":"10.1002/psc.70012","DOIUrl":"https://doi.org/10.1002/psc.70012","url":null,"abstract":"<div>\u0000 \u0000 <p>The discovery of novel candidate molecules that may transform cancer treatment carries significant clinical implications. Codesane (COD), an 18-amino acid peptide extracted from the wild bee venom of <i>Colletes daviesanus</i>, is categorized as a cationic α-helical amphipathic antimicrobial peptide. COD, produced via solid-phase peptide synthesis, displayed significant antitumor activity in vitro. However, its application as a drug is restricted by conformational flexibility, poor serum stability, and low selectivity. This research focused on designing, synthesizing, and evaluating a series of stapled COD derivatives by all-hydrocarbon stapling strategy. Compared to the original peptide COD, several of these stapled derivatives showed significant enhancements in α-helicity, serum resistance, antitumor activity, and cell selectivity. Significantly, the stapled derivative COD-5, which possesses high helicity, good serum stability, and favorable selectivity, shows promising potential for novel antitumor drug development, whereas COD-3, characterized by high selectivity and good antitumor activity, serves as a preferred candidate for novel breast cancer therapeutic drugs. These findings provide a solid foundation for developing innovative and highly effective antitumor therapies.</p>\u0000 </div>","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 7","pages":""},"PeriodicalIF":1.8,"publicationDate":"2025-05-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144117871","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

Antibody Labeling With FITC Facilitates Controlled Release From Peptide Hydrogels Bearing Fc-Binding Motifs 用FITC标记抗体有助于从含有fc结合基序的肽水凝胶中控制释放

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2025-05-21 DOI: 10.1002/psc.70032

Tania L. Lopez-Silva, Joel P. Schneider

{"title":"Antibody Labeling With FITC Facilitates Controlled Release From Peptide Hydrogels Bearing Fc-Binding Motifs","authors":"Tania L. Lopez-Silva, Joel P. Schneider","doi":"10.1002/psc.70032","DOIUrl":"https://doi.org/10.1002/psc.70032","url":null,"abstract":"<div>\u0000 \u0000 <p>Controlled release systems can enhance the efficacy of therapeutic antibodies, particularly for subcutaneous delivery where high or frequent doses are needed. Herein, we designed a peptide hydrogel that displays the binding motif HWRGWV, which targets the Fc-region of IgG. Release studies of FITC-labeled IgG from gel formulations demonstrated slow-release dependent on the Fc-binding motif's content as expected. However, the slow-release profile was diminished when using unlabeled IgG or the antibody Cetuximab, which lacks FITC. This observation and subsequent experiments show that the FITC label directly interacts with the Fc-binding motif displayed from the peptide nanofiber network to modulate release. Further, hydrogels bearing a scrambled version of the Fc-binding motif provide a similar slow-release profile for IgG-FITC but fast release for unlabeled antibodies, indicating that FITC binding of the Fc-binding motif is not specific in nature. Rather, nonspecific electrostatic and aromatic interactions most likely dictate binding and the observed slow-release kinetics of antibody from the gel. This work highlights the importance of considering fluorophore interactions when developing systems for the controlled release of antibodies and more importantly suggests that fluorophores can be used as affinity tags to control the release of protein from hydrogels with possible applications in theragnostic delivery.</p>\u0000 </div>","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 7","pages":""},"PeriodicalIF":1.8,"publicationDate":"2025-05-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144108938","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

Peptide-Based Catalyst Mimicking Hydrolase Enzyme 肽基催化剂模拟水解酶

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2025-05-21 DOI: 10.1002/psc.70031

Kalpana Kumari, Vivek Prakash, Naveen Kumar, Vibin Ramakrishnan

引用次数: 0

Identification of Potent Cell Penetrating, Nontoxic Peptides for Inhibiting MDM2–p53 Interactions: Characterization of Anticancer Peptides via Molecular Dynamics Simulations 鉴定有效的细胞穿透，无毒肽抑制MDM2-p53相互作用：表征抗癌肽通过分子动力学模拟

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2025-05-21 DOI: 10.1002/psc.70033

Pradeep Pant, Aman Sehgal, Tushar Gupta, Pradeep Sharma

{"title":"Identification of Potent Cell Penetrating, Nontoxic Peptides for Inhibiting MDM2–p53 Interactions: Characterization of Anticancer Peptides via Molecular Dynamics Simulations","authors":"Pradeep Pant, Aman Sehgal, Tushar Gupta, Pradeep Sharma","doi":"10.1002/psc.70033","DOIUrl":"https://doi.org/10.1002/psc.70033","url":null,"abstract":"<div>\u0000 \u0000 <p>Inhibiting MDM2–p53 interactions is a crucial therapeutic strategy in cancer treatment, as it can restore the tumor suppressor activity of p53 and inhibit tumor progression. Peptide inhibitors have shown promise in targeting this interaction; however, their optimization for in vivo use often encounters challenges, particularly in cellular uptake. The present study addresses this limitation by identifying cell-penetrating peptides (CPPs) that are predicted to be nontoxic to humans and capable of inhibiting the MDM2–p53 interaction. We utilized a comprehensive CPP database to extract unmodified peptides, focusing on those predicted to be nontoxic. Selected candidates were subjected to molecular docking followed by 500-ns all-atom explicit-solvent molecular dynamics (MD) simulations, performed in triplicates, to evaluate their binding stability and affinity with MDM2. Binding affinity calculations using MM-PBSA, AREA AFFINITY, and PRODIGY revealed that two peptides consistently exhibited stable binding to MDM2 and demonstrated higher affinity compared with the p53 reference fragment. These peptides not only maintained favorable interactions throughout the simulations but also showed strong potential to disrupt MDM2–p53 binding and reactivate p53 function. The findings highlight these peptides as promising nontoxic anticancer agents and provide a strong foundation for the development of peptide-based therapeutics targeting the MDM2–p53 interaction.</p>\u0000 </div>","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 7","pages":""},"PeriodicalIF":1.8,"publicationDate":"2025-05-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144100580","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

Synthesis of Diastereomerically Pure Cetrorelix Acetate by Using Fmoc Solid-Phase Peptide Synthesis (SPPS) Strategy: A Commercially Viable Approach Fmoc固相肽合成（SPPS）策略合成非对映体纯醋酸头孢瑞克：一种可行的商业方法

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2025-05-19 DOI: 10.1002/psc.70030

Kiran Aluri, Srinivas Basavoju, Jagadeesh B. Rangisetty, Manik R. Pullagurla, Bhaskar R. Pitta

{"title":"Synthesis of Diastereomerically Pure Cetrorelix Acetate by Using Fmoc Solid-Phase Peptide Synthesis (SPPS) Strategy: A Commercially Viable Approach","authors":"Kiran Aluri, Srinivas Basavoju, Jagadeesh B. Rangisetty, Manik R. Pullagurla, Bhaskar R. Pitta","doi":"10.1002/psc.70030","DOIUrl":"https://doi.org/10.1002/psc.70030","url":null,"abstract":"<div>\u0000 \u0000 <p>In the synthesis of cetrorelix via solid-phase peptide synthesis (SPPS) employing the Fmoc strategy, the racemization of L-arginine and L-serine was effectively minimized to below 0.5%. This reduction was achieved using the coupling agent HATU, the additive HOBt or HOAt, and the base TMP. Racemization was observed during the coupling of Fmoc-L-arginine(Pbf) and Fmoc-O-<i>tert</i>-butyl-L-serine on Rink Amide AM resin. A gradient reversed-phase high-performance liquid chromatography (RP-HPLC) method was developed for the separation of all the structurally closely related cetrorelix isomers. Optimized RP-HPLC conditions identified D-arginine and D-serine isomeric impurities as the closest eluting peaks to the main cetrorelix peak. Controlling these impurities to the lowest possible levels is essential for developing an efficient preparative HPLC purification process for the commercial production of cetrorelix. This stringent control ensures that the final product meets the high standards required for commercial production and therapeutic use.</p>\u0000 </div>","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 6","pages":""},"PeriodicalIF":1.8,"publicationDate":"2025-05-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144085432","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

Discovery of Bioactive Peptides Through Peptide Scanning 通过肽扫描发现生物活性肽

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2025-05-10 DOI: 10.1002/psc.70029

Debora Iaculli, Steven Ballet

{"title":"Discovery of Bioactive Peptides Through Peptide Scanning","authors":"Debora Iaculli, Steven Ballet","doi":"10.1002/psc.70029","DOIUrl":"https://doi.org/10.1002/psc.70029","url":null,"abstract":"<div>\u0000 \u0000 <p>Therapeutic peptides targeted at various diseases are becoming increasingly relevant for the pharmaceutical industry. Several of these drugs were originally designed by mimicking a segment of a protein of interest. As such, protein mimicry represents a promising strategy both in immunology, for the identification of B- and T-cell epitopes, as well as for the modulation of protein activity, including the disruption of protein–protein interactions (PPIs) and the interference with biological or pathological cellular functions. Several methods have been developed to pinpoint the (binding) epitopes of a protein or the regions responsible for biological activity. One of such strategies is the scanning of the protein or selected domains with synthetic overlapping peptides. As the mechanism of action of a mimetic peptide can be similar to that of the whole protein, this method offers a powerful tool for the investigation of protein function, along with providing a solid basis for the development of therapeutic candidates. This review gives a general overview of different applications of the peptide scanning methodology, describing a comparison of the preparation and use of solid-phase libraries (peptide arrays) with isolated peptide libraries and highlighting their strengths and most common applications.</p>\u0000 </div>","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 6","pages":""},"PeriodicalIF":1.8,"publicationDate":"2025-05-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143930219","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

Cytosolic Delivery of Functional Ubiquitin 功能性泛素的胞质递送

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2025-05-08 DOI: 10.1002/psc.70026

JoLynn B. Giancola, Aniekan Okon, Yanfeng Li, Eric R. Strieter, Ronald T. Raines

引用次数: 0

Synthesis of Stylissamide B, a Pro-Rich Cyclic Heptapeptide Isolated From the Marine Sponge Stylissa caribica 从加勒比海海绵体中分离的亲富环七肽花柱酰胺B的合成

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2025-05-07 DOI: 10.1002/psc.70028

Yitong Li, Hanyu Ling, Kenta Teruya, Hiroyuki Konno

引用次数: 0

In Vivo Evaluation of Pam2Cys-Modified Cancer-Testis Antigens as Potential Self-Adjuvanting Cancer Vaccines pam2cys修饰的癌睾丸抗原作为潜在的自佐剂癌症疫苗的体内评价

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2025-05-06 DOI: 10.1002/psc.70022

Salwa Aljohani, Alex G. Edmonds, Valeria Castelletto, Jani Seitsonen, Ian W. Hamley, Peter Symonds, Victoria A. Brentville, Lindy G. Durrant, Nicholas J. Mitchell

引用次数: 0

Antimicrobial and Potent Anti-Biofilm Properties of Rationally Designed α-Helix Antimicrobial Peptides 合理设计α-螺旋抗菌肽的抗菌和强效抗生物膜性能

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2025-05-06 DOI: 10.1002/psc.70027

Motasim Ismael, Khayeli Juliah, Madivoli Edwin

{"title":"Antimicrobial and Potent Anti-Biofilm Properties of Rationally Designed α-Helix Antimicrobial Peptides","authors":"Motasim Ismael, Khayeli Juliah, Madivoli Edwin","doi":"10.1002/psc.70027","DOIUrl":"https://doi.org/10.1002/psc.70027","url":null,"abstract":"<div>\u0000 \u0000 <p>The antimicrobial resistance (AMR) crisis represents a significant global threat. Unlike traditional antibiotics, antimicrobial peptides offer a promising pathway because of their primary mechanisms. This study aimed to evaluate and rationally design novel AMPs based on tobacco nectar's AMP (Pep 6) to combat antibiotic resistance issues. Substitution and truncation of some amino acids were applied. Four peptides, KF19, KF16, LK16, and LR16, were designed with enhanced net charge hydrophobicity. They were evaluated for their in vitro antibacterial activity. However, only promising AMPs were further evaluated for their hemolytic activity, time-killing kinetics, mode of action, and anti-biofilm properties. The results showed that only KF19 and LR16 have potent activity against <i>Staphylococcus aureus</i> ATCC25923 and resistant isolates with MIC values from 7.81 to 15.62 μg/mL. Hemolysis ratios were 2.38% and 2.24% at 125 μg/mL for KF19 and LR16, respectively. Both peptides were able to kill <i>S. aureus</i> ATCC25923 within 2 h. SEM results showed their ability to target the cell membrane. Both peptides destroyed the <i>S. aureus</i> biofilms significantly at 62.5 and 125 μg/mL (**<i>p</i> < 0.01, ***<i>p</i> < 0.001, ****<i>p</i> < 0.0001). This study supported rational design in developing new antibacterial agents and demonstrated the therapeutic potency of novel peptides that could solve the resistance issues.</p>\u0000 </div>","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 6","pages":""},"PeriodicalIF":1.8,"publicationDate":"2025-05-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143909184","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