Journal of Peptide Science最新文献_第6页

Examining Farnesyltransferase Interaction With Cell-Permeable CaaX Peptides and the Role of the CaaX Motif in Biological Activity 法尼基转移酶与细胞渗透性CaaX肽的相互作用及CaaX基序在生物活性中的作用

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2025-03-10 DOI: 10.1002/psc.70009

Merlin Klußmann, Jan Reuter, Christian Werner, Ines Neundorf

{"title":"Examining Farnesyltransferase Interaction With Cell-Permeable CaaX Peptides and the Role of the CaaX Motif in Biological Activity","authors":"Merlin Klußmann, Jan Reuter, Christian Werner, Ines Neundorf","doi":"10.1002/psc.70009","DOIUrl":"https://doi.org/10.1002/psc.70009","url":null,"abstract":"Recently, we presented cell-permeable CaaX peptides as versatile tools to study intracellular prenylation of proteins. These peptides consist of a cell-penetrating peptide (CPP) and a C-terminal CaaX motif derived from Ras proteins and demonstrated high cellular accumulation and the ability to influence Ras signaling in cancerous cells. Here, we aimed to gain a deeper insight into how such cell-permeable CaaX peptides, particularly the KRas4B-derived CaaX-1 peptide, interact with farnesyltransferase (FTase) and likely influence further intracellular processes. We show that CaaX-1 is farnesylated by FTase ex cellulo and that an intact CaaX motif is required for modification. A competition experiment revealed a slower farnesylation of CaaX-1 by FTase compared to a CaaX motif-containing control peptide. CaaX-1 inhibited farnesylation of this control peptide at considerably lower concentrations; thus, a higher affinity for FTase is hypothesized. Notably, AlphaFold3 not only predicted interactions between CaaX-1 and FTase but also suggested interactions between the peptide and geranylgeranyltransferase type I. This finding encourages further investigation, as cross-prenylation is a well-known drawback of FTase inhibitors. Our results are further evidence for the usefulness of CaaX peptides as tools to study and manipulate the prenylation of proteins. They offer real potential for the development of novel inhibitors targeting the prenylation pathway.","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 4","pages":""},"PeriodicalIF":1.8,"publicationDate":"2025-03-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/psc.70009","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143594867","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

Solid-Phase Synthesis of Peptide Hydrazides: Moving Toward Green Chemistry 肽酰肼的固相合成：走向绿色化学

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2025-03-06 DOI: 10.1002/psc.70010

Maria Leko, Polina Filippova, Karin Rustler, Thomas Bruckdorfer, Sergey Burov

{"title":"Solid-Phase Synthesis of Peptide Hydrazides: Moving Toward Green Chemistry","authors":"Maria Leko, Polina Filippova, Karin Rustler, Thomas Bruckdorfer, Sergey Burov","doi":"10.1002/psc.70010","DOIUrl":"https://doi.org/10.1002/psc.70010","url":null,"abstract":"<div>\u0000 \u0000 Peptide hydrazides are widely applied as precursors of peptide thioesters, valuable building blocks for the synthesis of proteins by native chemical ligation. In addition, they can be applied for the selective modification of cargo or carrier molecules using hydrazone ligation technique. In this work, we describe key aspects of solid phase synthesis of peptide hydrazides on hydrazine 2CT and hydrazone resin. Special attention is paid to the optimization of synthetic procedures using “preferred” and “usable” organic solvents. Thus, optimization of 2-CTC resin loading with Fmoc-hydrazine permits to reduce reagents consumption and avoid DMF and DCM application. The final products can be released from the polymer support with simultaneous BOC removal with 5% HCl (aq) in acetone. Although this protocol demands subsequent peptide deprotection to remove other protecting groups, it benefits of significantly reduced TFA consumption. Because of improved stability in acidic conditions and the possibility of selective Mtt removal and peptide cleavage in green solvents, hydrazone resin can be considered as a useful alternative for peptide hydrazides synthesis. Obtained results can simplify the synthesis of peptide building blocks for native chemical ligation using CMR-free reagents and solvents.\u0000 </div>","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 4","pages":""},"PeriodicalIF":1.8,"publicationDate":"2025-03-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143554572","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

Preventing Protein Self-Association Through Strategic Covalent Modification 通过战略性共价修饰防止蛋白质自结合

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2025-03-06 DOI: 10.1002/psc.70008

Swetha Chintala, Simon H. Friedman

{"title":"Preventing Protein Self-Association Through Strategic Covalent Modification","authors":"Swetha Chintala, Simon H. Friedman","doi":"10.1002/psc.70008","DOIUrl":"https://doi.org/10.1002/psc.70008","url":null,"abstract":"<div>\u0000 \u0000 Protein self-interaction leading to aggregation is a major challenge facing protein pharmaceuticals. It leads to a range of problems, including increases in immunogenicity and loss of activity. In this work, we describe an approach for blocking or antagonizing the quaternary interactions that drive self-association. We applied the approach to glucagon, a therapeutic peptide known for its propensity to form fibrils due to self-interaction. We synthesized a regio-pure common feedstock that allowed easy modification with potential blocking peptides that represented a range of chemical types (anionic, cationic, polar, and nonpolar). From these synthesized materials, we identified two modified glucagons that showed significant stabilization against fibril formation compared with unmodified glucagon. This was confirmed by three complementary biophysical techniques. Both successful modifications introduced excess net charge to glucagon, consistent with overall electrostatic repulsion being at the root of the observed fibrillation resistance. This approach can potentially be applied to other therapeutic proteins that suffer from the problems associated with self-association.\u0000 </div>","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 4","pages":""},"PeriodicalIF":1.8,"publicationDate":"2025-03-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143555019","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

Identification and Characterization of a Novel GAPDH-Derived Antimicrobial Peptide From Jellyfish 一种新型水母gapdh衍生抗菌肽的鉴定与表征

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2025-03-05 DOI: 10.1002/psc.70011

Jingwen Liu, An Li, Yueyue Li, Jing Li, Xiaoyu Geng, Junyi Wan, Qianqian Lu, Qingqing Wang, Mingke Wang, Jishun Yang

{"title":"Identification and Characterization of a Novel GAPDH-Derived Antimicrobial Peptide From Jellyfish","authors":"Jingwen Liu, An Li, Yueyue Li, Jing Li, Xiaoyu Geng, Junyi Wan, Qianqian Lu, Qingqing Wang, Mingke Wang, Jishun Yang","doi":"10.1002/psc.70011","DOIUrl":"https://doi.org/10.1002/psc.70011","url":null,"abstract":"Marine organisms serve as a rich source of bioactive natural compounds, including antimicrobial agents. Jellyfish, which are ancient marine invertebrates with hundreds of millions of years of evolutionary history, have been in continuous contact with a diverse array of pathogenic microorganisms from seawater, which may give rise to a distinctive innate immune system and related defensive molecules. However, it is difficult and inefficient to isolate active ingredients directly from jellyfish for enrichment, though few jellyfish-sourced antimicrobial peptides (AMPs) have been reported. In this study, we utilized transcriptomic big data with bioinformatic tools to dig deeper into potential antimicrobial components in jellyfish, and identified a new AMP JFP-2826 from Rhopilema esculentum. The 20-mer peptide exhibited an alpha-helix structure and showed antimicrobial activity against selected bacterial strains; more importantly, JFP-2826 demonstrated good selectivity for marine-specific Vibrio including Vibrio vulnificus. Sequence analysis of the full-length protein of JFP-2826 revealed that it is derived from the housekeeping gene glyceraldehyde-3-phosphate dehydrogenase (GAPDH), which is probably produced through enzymatic cleavage of the N-terminal fragment. This suggests that GAPDH of jellyfish might have a newly discovered antimicrobial-related function that is conducted by releasing JFP-2826-like cryptic peptides. JFP-2826 can be subjected to further structural modifications and optimizations to potentially become a potent lead peptide for the development of novel antimicrobial drugs treating infections of marine pathogens.","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 4","pages":""},"PeriodicalIF":1.8,"publicationDate":"2025-03-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/psc.70011","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143554391","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

Cancer-Targeting Peptides Functionalized With Polyarginine Enables GRP78-Dependent Cell Uptake and siRNA Delivery Within the DU145 Prostate Cancer Cells 用聚精氨酸功能化的癌症靶向肽能够在DU145前列腺癌细胞中实现grp78依赖性细胞摄取和siRNA递送

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2025-02-18 DOI: 10.1002/psc.70007

George Hilan, Grace Daniel, Filiz Collak, David Sabatino, William G. Willmore

{"title":"Cancer-Targeting Peptides Functionalized With Polyarginine Enables GRP78-Dependent Cell Uptake and siRNA Delivery Within the DU145 Prostate Cancer Cells","authors":"George Hilan, Grace Daniel, Filiz Collak, David Sabatino, William G. Willmore","doi":"10.1002/psc.70007","DOIUrl":"https://doi.org/10.1002/psc.70007","url":null,"abstract":"This study investigated a peptide-based GRP78-targeting strategy for short-interfering (si) RNA delivery in cancer cells. Synthetic fluorescein-labeled amphiphilic peptides composed of the hydrophobic cell surface (cs) GRP78-targeting and hydrophilic, polycationic arginine-rich cell penetrating peptides demonstrated GRP78-dependent cell uptake in the DU145 prostate cancer cells, and to a lesser extent in the non-cancerous human lung fibroblast WI-38 cell line. Mechanistic studies revealed energy-dependent GRP78 receptor-mediated endocytosis of the GRP78-targeting peptide with polyarginine (W1-R9). The cytosolic accumulation of this peptide underscored its potential utility in siRNA delivery. Peptide:siRNA complexes formed stably condensed nanoparticles, with calcium functioning as an ionic stabilizer and additive promoting endosomal siRNA escape for RNA interference (RNAi) activity. Preliminary peptide-based siRNA transfections in the DU145 cells demonstrated that GRP78 knockdown led to an interplay in between pro-survival and cell death outcomes under ER stress induction. Thus, the GRP78-targeting polyarginine peptides enables efficient cell uptake for specific siRNA delivery in the DU145 cells. This class of bio-active synthetic peptides is important for the investigation of cancer biology, leading to the innovation of cancer-targeted gene delivery and therapy approaches.","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 3","pages":""},"PeriodicalIF":1.8,"publicationDate":"2025-02-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/psc.70007","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143439131","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

Versatile Features of an Antibody Mimetic Peptide and Its Variants 一种抗体模拟肽及其变体的多用途特性

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2025-02-17 DOI: 10.1002/psc.70005

Simon Dolles, Simon Leukel, Sabrina Gensberger-Reigl, Anette Rohrhofer, Lena Rauch-Wirth, Kübra Kaygisiz, Christopher V. Synatschke, Jan Münch, Barbara Schmidt, Monika Pischetsrieder, Jutta Eichler

{"title":"Versatile Features of an Antibody Mimetic Peptide and Its Variants","authors":"Simon Dolles, Simon Leukel, Sabrina Gensberger-Reigl, Anette Rohrhofer, Lena Rauch-Wirth, Kübra Kaygisiz, Christopher V. Synatschke, Jan Münch, Barbara Schmidt, Monika Pischetsrieder, Jutta Eichler","doi":"10.1002/psc.70005","DOIUrl":"https://doi.org/10.1002/psc.70005","url":null,"abstract":"Antibody mimetic peptides have evolved as versatile tools for biomedical applications, based on their ability to interfere with protein–protein interactions. We had previously designed a functional mimic of the broadly neutralizing HIV-1 antibody b12 that recognizes the CD4 binding site of the HIV-1 envelope glycoprotein gp120. The molecular details of the interaction of a linear variant of this peptide (H1H3s) with gp120 have now been characterized through cross-linking mass spectrometry, confirming the proposed involvement of the CD4 binding site of gp120 in the interaction. In addition, a variant of the b12 mimetic peptide composed mostly of D-amino acids was shown to be stable towards proteolytic degradation, while the binding and HIV-1 neutralizing properties were largely preserved. Furthermore, a peptide variant in which aspartate residues were replaced with lysine was shown to strongly enhance infection of cells with HIV-1 and GALV glycoprotein pseudotyped viral vectors, respectively, introducing this peptide as a tool to facilitate retroviral gene transfer. Collectively, the presented results highlight the versatile potential therapeutic and gene transfer applications of H1H3s and its variants in particular, as well as antibody mimetic peptides in general.","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 3","pages":""},"PeriodicalIF":1.8,"publicationDate":"2025-02-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/psc.70005","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143431132","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

IAMPDB: A Knowledgebase of Manually Curated Insects-Derived Antimicrobial Peptides IAMPDB：人工筛选昆虫来源的抗菌肽知识库

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2025-02-11 DOI: 10.1002/psc.70006

Rajat Kumar Mondal, Prabhat Tripathi, Rudra Prasad Mondal, Debarup Sen, Ankish Arya, Debayan Karmakar, Oshin Pal, Avijit Dey, Sintu Kumar Samanta

{"title":"IAMPDB: A Knowledgebase of Manually Curated Insects-Derived Antimicrobial Peptides","authors":"Rajat Kumar Mondal, Prabhat Tripathi, Rudra Prasad Mondal, Debarup Sen, Ankish Arya, Debayan Karmakar, Oshin Pal, Avijit Dey, Sintu Kumar Samanta","doi":"10.1002/psc.70006","DOIUrl":"https://doi.org/10.1002/psc.70006","url":null,"abstract":"<div>\u0000 \u0000 Insects, a majority of animal species, rely on innate immunity and antimicrobial peptides (AMPs), which are a part of their innate immunity, to combat diverse parasites and pathogens. These peptides have applications ranging from agriculture to antimicrobial resistance (AMR). However, there is a lack of a specialized database, prompting the development of the Insect Antimicrobial Peptide Database (IAMPDB) as a pioneering comprehensive Knowledgebase dedicated to insect-derived antimicrobial peptides (IAMPs), serving as a resource for researchers and industry professionals. Curated from UniProt and associated literature(s), IAMPDB currently houses 438 curated entries of IAMPs from various insect species, spanning 10 taxonomical orders of insects. Each entry is meticulously annotated with details on peptide sequence, source organism, activities, physicochemical properties, and more. IAMPDB offers a user-friendly interface with diverse search options, interactive visualizations, and links to external databases; advanced tools, including a peptide sequence alignment toolbox and a peptide feature calculation toolbox, facilitating sequence alignment, physicochemical property calculation, and in-depth analysis. The knowledgebase is accessible online (at URL https://bblserver.org.in/iampdb/).\u0000 </div>","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 3","pages":""},"PeriodicalIF":1.8,"publicationDate":"2025-02-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143389140","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

Regulatory Guidelines for the Analysis of Therapeutic Peptides and Proteins 治疗性多肽和蛋白质分析的监管指南

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":"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.","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 anabaenopeptin的合成及其n端序列多样性研究

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 靶向癌细胞表面蛋白的噬菌体显示肽的评估：一项全面的分子对接研究

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 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.\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