Journal of Peptide Science最新文献_第7页

Self-Assembly of a Conjugate of Lipoic Acid With a Collagen-Stimulating Pentapeptide Showing Cytocompatibility and Wound Healing Properties, and Chemical and Photolytic Disassembly 具有细胞相容性和伤口愈合特性的硫辛酸与胶原刺激五肽偶联物的自组装，以及化学和光解分解

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 KALA和REV细胞穿透肽在体外/体内传递HPV多表位DNA结构的效力研究。

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

The Potential Effect of Endogenous Antimicrobial Peptides in Cancer Immunotherapy and Prevention 内源性抗菌肽在肿瘤免疫治疗和预防中的潜在作用。

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2024-12-23 DOI: 10.1002/psc.3664

Tuan Hiep Tran, Thanh Huong Le, Thi Thu Phuong Tran

{"title":"The Potential Effect of Endogenous Antimicrobial Peptides in Cancer Immunotherapy and Prevention","authors":"Tuan Hiep Tran, Thanh Huong Le, Thi Thu Phuong Tran","doi":"10.1002/psc.3664","DOIUrl":"10.1002/psc.3664","url":null,"abstract":"<div>\u0000 \u0000 <p>Antimicrobial peptides (AMPs) are crucial constituents of inherent immunity and serve as vital components of human host defense, playing a pivotal role in combating invading microbial pathogens. Beyond their antimicrobial functions, AMPs also exhibit various other biological activities including apoptosis induction, wound healing promotion, and immune modulation. These peptides are found in various exposed tissues or surfaces throughout the body, such as eyes, skin, mouth, ears, respiratory tract, lungs, digestive, and urinary system. Additionally, certain AMPs such as LL-37, HNP, and lactoferrin have shown potential as candidates for anticancer activity. Given the limited selectivity between normal and cancer cells exhibited by many current immunotherapeutic agents, the inherent properties of AMPs make them promising candidates for cancer treatment. Their abundance, bioavailability, safety profile, efficiency, and harmony with the host immune system position them as attractive tools in the fight against cancer. This review is aimed at exploring the potential anticancer properties of AMPs and elucidating their relationship with immunology and cancer immunotherapy.</p>\u0000 </div>","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 2","pages":""},"PeriodicalIF":1.8,"publicationDate":"2024-12-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142882326","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

Norleucine Substitution Enhances Self-Assembly of a Lanthanide-Binding Polypeptide Coiled Coil 正亮氨酸取代可增强镧系元素结合多肽盘绕线圈的自组装能力

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2024-12-20 DOI: 10.1002/psc.3665

Diego B. Sarte, Aaron Joseph L. Villaraza

{"title":"Norleucine Substitution Enhances Self-Assembly of a Lanthanide-Binding Polypeptide Coiled Coil","authors":"Diego B. Sarte, Aaron Joseph L. Villaraza","doi":"10.1002/psc.3665","DOIUrl":"https://doi.org/10.1002/psc.3665","url":null,"abstract":"<div>\u0000 \u0000 <p>A de novo lanthanide-binding coiled-coil polypeptide (MB1–2) was previously reported to self-assemble into a trimeric complex upon addition of Tb<sup>3+</sup> with a micromolar range dissociation constant. This study examines the effect of substitution of hydrophobic residues in heptad repeats of MB1–2 on the thermodynamic stability of the resulting Tb-peptide complex. Substitution of isoleucine to norleucine in each heptad repeat was assessed considering the greater accessible surface area of the latter and predicted increased hydrophobic interaction. Job's method of continuous variation using circular dichroism spectroscopy suggests a trimeric structure for the analog complex equivalent to that formed by MB1–2. The dissociation constant and CD spectra suggest that complex formation in the analog is more favorable as a result of ligand preorganization. In addition, thermal denaturation suggests greater stability of the Tb-MB1–2 Nle complex in comparison to the parent Tb-MB1–2. These results indicate improved stability of the complex class can be achieved through heptad repeat amino acid substitutions that increase peptide interchain interaction.</p>\u0000 </div>","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 2","pages":""},"PeriodicalIF":1.8,"publicationDate":"2024-12-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142861902","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

cDNA Display Selection of Interacting Peptide Ligands of the Guanylate Cyclase C Receptor 鸟苷酸环化酶C受体相互作用肽配体的cDNA展示选择。

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2024-12-10 DOI: 10.1002/psc.3663

Eri Ochiai, Yuki Takahashi, Shota Inokuchi, Akie Sumiya, Makoto Hasegawa

{"title":"cDNA Display Selection of Interacting Peptide Ligands of the Guanylate Cyclase C Receptor","authors":"Eri Ochiai, Yuki Takahashi, Shota Inokuchi, Akie Sumiya, Makoto Hasegawa","doi":"10.1002/psc.3663","DOIUrl":"10.1002/psc.3663","url":null,"abstract":"<div>\u0000 \u0000 <p>Guanylate cyclase C (GC-C), a receptor expressed on the apical membrane of intestinal mucosal cells, is activated by heat-stable enterotoxin (STa) produced by enterotoxigenic <i>Escherichia coli</i>, as well as the endogenous ligands guanylin and uroguanylin. In this study, novel peptides that interact with GC-C were generated using the cDNA display method, and their binding affinity and biological activity were evaluated. While the linear peptide library did not yield peptides with sufficient affinity for GC-C, three cyclic peptides (GCC-P1, GCC-P2, and GCC-P3), each containing two cysteine residues within a 15-residue sequence, were obtained from a cyclic peptide library containing nine-residue random sequences. GC-P2 exhibited significant binding affinity in Biacore assays, although the affinity was lower than those reported for known ligands. Notably, GCC-P2 and GCC-P3 demonstrated enhanced cGMP activity when used in combination with linaclotide. However, the agonist activity of these peptides was minimal, indicating that further modifications may be necessary to develop them for clinical applications. This study successfully extracted consensus sequences of peptide motifs that bind to GC-C from a highly diverse nine-residue random sequence library, which provides fundamental insights for the discovery and optimization of novel GC-C ligands.</p>\u0000 </div>","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 1","pages":""},"PeriodicalIF":1.8,"publicationDate":"2024-12-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142807438","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