Journal of Peptide Science最新文献_第3页

Chemical Synthesis of Crustacean Insulin-Like Peptide Using a Novel Method to Prevent Methionine Oxidation During Solid Phase Peptide Synthesis 一种防止甲硫氨酸在固相合成过程中氧化的新方法合成甲壳类胰岛素样肽

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2025-07-11 DOI: 10.1002/psc.70042

Hidekazu Katayama, Naoaki Tsutsui

{"title":"Chemical Synthesis of Crustacean Insulin-Like Peptide Using a Novel Method to Prevent Methionine Oxidation During Solid Phase Peptide Synthesis","authors":"Hidekazu Katayama, Naoaki Tsutsui","doi":"10.1002/psc.70042","DOIUrl":"https://doi.org/10.1002/psc.70042","url":null,"abstract":"The oxidation of Met residue(s) in peptides and proteins is sometimes found in solid phase peptide synthesis (SPPS). In this study, in order to develop a method to prevent the oxidation of Met during SPPS, various sulfide compounds were added to the solvent and the oxidation rate was measured. As a result, it was found that tetrahydrothiophene (THT) was most efficient for reducing the extent of Met oxidation. THT tended to prevent the oxidation of Met in a concentration-dependent manner, although the oxidation of Met could not be completely prevented even at a concentration of 20% (v/v). On the other hand, when the SPPS in the presence of THT and then reduction of Met(O) to Met with NH4I were performed, the yield was much improved. These results indicate that the combination of preventing oxidation with THT and reducing Met with NH4I is effective for the synthesis of peptides containing Met residue(s). Using the method established here, we could synthesize an insulin-like peptide from the kuruma shrimp. This method is likely to be applicable to the synthesis of various Met-containing peptides.","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 8","pages":""},"PeriodicalIF":1.8,"publicationDate":"2025-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/psc.70042","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144606732","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

Influence of Buffering Capacity, pH, and Temperature on the Stability of Semaglutide: A Preformulation Study 缓冲容量、pH和温度对西马鲁肽稳定性影响的预制剂研究

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2025-07-09 DOI: 10.1002/psc.70039

Adarsh Malgave, Sideequl Akbar, Ayushi Tiwari, Shamal Hande, Anumol Joseph, Rajkumar Malayandi

{"title":"Influence of Buffering Capacity, pH, and Temperature on the Stability of Semaglutide: A Preformulation Study","authors":"Adarsh Malgave, Sideequl Akbar, Ayushi Tiwari, Shamal Hande, Anumol Joseph, Rajkumar Malayandi","doi":"10.1002/psc.70039","DOIUrl":"https://doi.org/10.1002/psc.70039","url":null,"abstract":"<div>\u0000 \u0000 Therapeutic peptides' physical and chemical stability is of significant interest to the pharmaceutical industry. This study examines the effects of pH, temperature, and buffer strength on semaglutide (SEMA) stability using two orthogonal stability-indicating reverse-phase high-performance liquid chromatography (RP-HPLC) methods. The findings aid in designing novel oral and long-acting injectable (LAI) SEMA formulations. Two RP-HPLC methods were developed and validated to separate SEMA and its degradants. Stability studies were conducted at 25°C, 40°C, and 55°C for 24 h in water, with extended studies at 5°C, 25°C, 40°C, 60°C, and 80°C. pH and buffer strength effects were assessed at 25°C and 40°C. SEMA remained stable for 3 h at 80°C. The results obtained from pH-dependent stability studies indicated that SEMA was relatively stable at pH 1.2 at 25°C and 40°C for a day. A higher extent of degradation was observed between the pH of 4.5–5.5; this is due to the isoelectric point of SEMA (pH 5.4), and hence, the finished product pH should be > 7.0. These findings highlight the critical influence of buffer, temperature, and pH on SEMA stability. The results obtained by this study would help develop both oral and LAI SEMA formulations.\u0000 </div>","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 8","pages":""},"PeriodicalIF":1.8,"publicationDate":"2025-07-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144589626","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

Photocatalytic Diselenide Contraction as a Tool for Site-Selective Isosteric Ubiquitylation 光催化二烯醛收缩作为位点选择性等构泛素化的工具

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2025-07-03 DOI: 10.1002/psc.70037

Herwig Weissinger, Moritz Urschbach, Luca Ferrari, Sascha Martens, Christian F. W. Becker

{"title":"Photocatalytic Diselenide Contraction as a Tool for Site-Selective Isosteric Ubiquitylation","authors":"Herwig Weissinger, Moritz Urschbach, Luca Ferrari, Sascha Martens, Christian F. W. Becker","doi":"10.1002/psc.70037","DOIUrl":"https://doi.org/10.1002/psc.70037","url":null,"abstract":"Ubiquitylation is a highly conserved post-translational modification (PTM) in eukaryotes, which serves as a critical regulatory mechanism for protein homeostasis, cellular transport, signal transduction pathways, and numerous other functions. The biological function of ubiquitylation is dictated predominantly by the topology of its linkage. Deciphering ubiquitin's complex biochemistry necessitates novel synthetic methods that deliver well-defined, biosimilar ubiquitylation. To this end, a semisynthetic strategy relying on the recombinant expression of ubiquitin combined with chemoselective photocatalytic diselenide contraction (PDC) was established to enable site-selective biomimetic selenalysine-linked ubiquitylation. The modification of ubiquitin with a C-terminal selenol was fine-tuned to avoid hydrolysis. The conditions of the PDC reaction, such as solvent composition, phosphine concentration, and irradiation, were optimized for efficient ubiquitylation of a Tau F derived peptide. Furthermore, it was demonstrated that the selenalysine linkage undergoes efficient cleavage by deubiquitylating enzymes, comparable to the native isopeptide linkage. The presented method expands the toolbox of site-selective ubiquitylation techniques. It is tolerant to many functional groups and will help to further elucidate the complexities of ubiquitylation.","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 8","pages":""},"PeriodicalIF":1.8,"publicationDate":"2025-07-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/psc.70037","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144551152","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

Toward a Green SPPS: The Use of an Innovative Mesoporous pDVB Support for Environmentally Friendly Solvents 迈向绿色SPPS：使用创新的介孔pDVB支持环保溶剂

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2025-06-30 DOI: 10.1002/psc.70038

Luana Lastella, Marco Zecca, Paolo Centomo, Karel Jeřábek, Fernando Formaggio, Ivan Guryanov, Antonio Ricci, Barbara Biondi

{"title":"Toward a Green SPPS: The Use of an Innovative Mesoporous pDVB Support for Environmentally Friendly Solvents","authors":"Luana Lastella, Marco Zecca, Paolo Centomo, Karel Jeřábek, Fernando Formaggio, Ivan Guryanov, Antonio Ricci, Barbara Biondi","doi":"10.1002/psc.70038","DOIUrl":"https://doi.org/10.1002/psc.70038","url":null,"abstract":"This study explores the use of a novel polymeric mesoporous support (pDVB) for solid-phase peptide synthesis (SPPS), with the aim of improving the efficiency and sustainability of the process. The pDVB support, functionalized with the Fmoc-Rink amide linker, offers advantages over conventional supports based on gel-type, lightly crosslinked polymer skeletons, particularly with regard to reduced reliance on swelling capacity, which allows the use of a wider range of solvents. The work focuses on greener and eco-friendly solvents such as TEP, ACN, IPA, and their mixtures with DMSO to replace toxic solvents such as DMF. The synthesis of two model peptide sequences, Fmoc-LLVF-NH2 and ACP(65–74), showed that pDVB-Rink performs better than a conventional-type Rink Amide MBHA support, especially when using environmentally friendly solvents. These results suggest that mesoporous pDVB-Rink is a promising solid support for SPPS to reduce the use of toxic solvents and to improve sustainability.","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 8","pages":""},"PeriodicalIF":1.8,"publicationDate":"2025-06-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/psc.70038","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144520229","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

Antimigratory and Antiproliferative Effects of the Brain-Targeted Peptide Conjugate PepH3-vCPP2319 on Triple Negative Breast Cancer Cell Cultures 脑靶向肽偶联物PepH3-vCPP2319对三阴性乳腺癌细胞培养的抗迁移和抗增殖作用

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2025-06-19 DOI: 10.1002/psc.70035

Catarina Gonçalves, Miguel A. R. B. Castanho, Marco Cavaco, Vera Neves

{"title":"Antimigratory and Antiproliferative Effects of the Brain-Targeted Peptide Conjugate PepH3-vCPP2319 on Triple Negative Breast Cancer Cell Cultures","authors":"Catarina Gonçalves, Miguel A. R. B. Castanho, Marco Cavaco, Vera Neves","doi":"10.1002/psc.70035","DOIUrl":"https://doi.org/10.1002/psc.70035","url":null,"abstract":"<div>\u0000 \u0000 Triple-negative breast cancer (TNBC) is an aggressive breast cancer subtype affecting mostly younger women with a poor 5-year overall survival. It is characterized by a high metastization rate, particularly to the brain, where the blood–brain barrier (BBB) hinders the pharmaceuticals delivery. New anticancer drugs able to inhibit cell migration are required to effectively prevent the development of metastasis. PepH3-vCPP2319 (AGILKRW(Ahx)WRRRYRRWRRRRRQRRRPRR-amide), consisting of the conjugation of the BBB peptide shuttle (BBBpS) PepH3 (AGILKRW-amide) to the anticancer peptide (ACP) vCPP2319 (WRRRYRRWRRRRRQRRRPRR-amide), was reported to have high anticancer activity (IC50 = 5.0 μM) toward highly aggressive TNBC cells (MDA-MB-231) paired with 2-fold increased accumulation in the brain when compared to unconjugated vCPP2319. Herein, we demonstrate that PepH3-vCPP2319 inhibits cell migration and proliferation in wound healing assays, outperforming the gold standard small chemical inhibitor, iCRT-3. The concentration required to inhibit cell migration is 10-fold lower for PepH3-vCPP2319 (0.5 μM) when compared with iCRT-3 (50 μM). Likewise, PepH3-vCPP2319 at 2.5 μM was more efficient in preventing cell proliferation when compared with 50 μM iCRT-3, with 45% reduction in spheroid diameter. This study sheds light on the antimetastatic potential of PepH3-vCPP2319 through abrogation of cell migration to distant sites, including the brain.\u0000 </div>","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 8","pages":""},"PeriodicalIF":1.8,"publicationDate":"2025-06-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144323343","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

π-Turns in Peptides: A Crystal-State Literature Survey 多肽中的π-旋：晶体文献综述

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2025-06-15 DOI: 10.1002/psc.70036

Barbara Biondi, Fernando Formaggio, Claudio Toniolo, Cristina Peggion, Marco Crisma

{"title":"π-Turns in Peptides: A Crystal-State Literature Survey","authors":"Barbara Biondi, Fernando Formaggio, Claudio Toniolo, Cristina Peggion, Marco Crisma","doi":"10.1002/psc.70036","DOIUrl":"https://doi.org/10.1002/psc.70036","url":null,"abstract":"The results of an analysis on the presence of π-turns, characterized by an i ← i + 5 C=O···H–N intramolecular hydrogen bond, in the X-ray diffraction structures of peptides are discussed. The survey returned a total of 55 π-turn occurrences in linear and cyclic peptides. π-Turns characterized by a helical conformation for residue i + 4, but with a screw sense opposite to that of the three preceding residues, are largely prevailing. They are often found at the C-end of incipient or fully developed α-helices, 310-helices, and mixed α-/310-helices, thus acting as a C-capping motif. However, the structures of two linear peptides and 15 cyclopeptides indicate that these types of π-turns can exist in isolation, without the support of a preceding helix. The frequent presence of additional intramolecular hydrogen bonds internal to the π-turn is also investigated. Cyclopeptides offered examples of two types of π-turns that have no parallel in the structures of proteins. Differently from proteins, π-turns characterized by helical ϕ, ψ sets of the same screw sense for all internal residues are hitherto unreported in the X-ray diffraction structures of peptides. A suggestion for the rational design in peptides/peptidomimetics of a π-turn featuring the screw-sense reversal of residue i + 4 is proposed.","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 7","pages":""},"PeriodicalIF":1.8,"publicationDate":"2025-06-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/psc.70036","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144292344","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

Phage Display–Selected Peptides: Research and Clinical Applications in Cancer Imaging 噬菌体展示选择肽：癌症成像的研究和临床应用

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2025-06-03 DOI: 10.1002/psc.70034

Atike Nur Cimen, Melis Hazal Porsuk, Ozlem Kutlu, Sibel Cetinel

引用次数: 0

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 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 Colletes daviesanus, 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.\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 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.\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