Journal of Peptide Science最新文献

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Relevance of amphiphilicity and helicity on the antibacterial action of a histatin 5-derived peptide 两亲性和螺旋性对组蛋白 5 衍生肽抗菌作用的影响
IF 1.8 4区 生物学
Journal of Peptide Science Pub Date : 2024-04-27 DOI: 10.1002/psc.3609
Cristina Peggion, Valeria Panetta, Luana Lastella, Fernando Formaggio, Antonio Ricci, Simona Oancea, Geta Hilma, Barbara Biondi
{"title":"Relevance of amphiphilicity and helicity on the antibacterial action of a histatin 5-derived peptide","authors":"Cristina Peggion,&nbsp;Valeria Panetta,&nbsp;Luana Lastella,&nbsp;Fernando Formaggio,&nbsp;Antonio Ricci,&nbsp;Simona Oancea,&nbsp;Geta Hilma,&nbsp;Barbara Biondi","doi":"10.1002/psc.3609","DOIUrl":"10.1002/psc.3609","url":null,"abstract":"<p>Peptide dhvar4, derived from the active domain of our salivary peptide histatin 5, bears a Phe residue in the middle of its hydrophilic face when folded into an α-helix. We then synthesized an analog with this Phe replaced by Lys and two analogs preserving Phe but bearing two and three α-aminoisobutyric acid (Aib) residues to stabilize the helical structure. The aim of this design was to verify which of the two features is more favorable to the biological activity. We performed a conformational study by means of circular dichroism and nuclear magnetic resonance, made antibacterial tests, and assessed the stability of the peptides in human serum. We observed that amphiphilicity is more important than helix stability, provided a peptide can adopt a helical conformation in a membrane-mimetic environment.</p>","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":null,"pages":null},"PeriodicalIF":1.8,"publicationDate":"2024-04-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140805748","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
Optimization of peptide synthesis time and sustainability using novel eco-friendly binary solvent systems with induction heating on an automated peptide synthesizer 在自动多肽合成器上使用新型环保二元溶剂系统和感应加热,优化多肽合成时间和可持续性
IF 1.8 4区 生物学
Journal of Peptide Science Pub Date : 2024-04-25 DOI: 10.1002/psc.3605
Lorenzo Pacini, Manoj Muthyala, Luisa Aguiar, Robert Zitterbart, Paolo Rovero, Anna Maria Papini
{"title":"Optimization of peptide synthesis time and sustainability using novel eco-friendly binary solvent systems with induction heating on an automated peptide synthesizer","authors":"Lorenzo Pacini,&nbsp;Manoj Muthyala,&nbsp;Luisa Aguiar,&nbsp;Robert Zitterbart,&nbsp;Paolo Rovero,&nbsp;Anna Maria Papini","doi":"10.1002/psc.3605","DOIUrl":"10.1002/psc.3605","url":null,"abstract":"<p>On December 12th, 2023, the European Commission took regulatory action to amend Annex XVII of REACH, imposing restrictions on the use of <i>N</i>,<i>N</i>-dimethylformamide (DMF) within the EU market owing to its high toxicity. Historically, DMF has been widely considered the gold standard for solid-phase peptide synthesis (SPPS). Being urgent to propose alternative solvents, we tested the suitability of non-hazardous neat and mixed solvents. Notably, binary solvent mixtures containing dimethyl sulfoxide as one of the solvent partners demonstrated high efficacy in solubilizing reagents while maintaining the desired swelling characteristics of common resins. A series of binary solvent mixtures were tested in automated SPPS, both at room temperature and high temperature, employing the PurePep® Chorus synthesizer, which enabled controlled induction heating between 25 and 90°C with oscillation mixing. The performances were assessed in challenging peptide sequences, i.e., ACP (65–74), and in longer and aggregating sequences like SARS-CoV-2 RBM (436–507) and β-amyloid (1–42). Furthermore, as part of the proposed sustainable approach to minimize the utilization of hazardous solvents, we coupled the novel PurePep EasyClean catch-and-release purification technology. This work, addressing regulatory compliance, emphasizes the crucial role of green chemistry in advancing safer and more environmentally friendly practices in SPPS.</p>","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":null,"pages":null},"PeriodicalIF":1.8,"publicationDate":"2024-04-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140805611","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
Investigating the impact of thiol reactivity and disulfide formation on cellular uptake of cell-permeable peptides 研究硫醇反应性和二硫化物的形成对细胞渗透肽吸收的影响
IF 1.8 4区 生物学
Journal of Peptide Science Pub Date : 2024-04-23 DOI: 10.1002/psc.3604
Merlin Klußmann, Katharina Stillger, Melina Ruppel, Coco-Louisa Sticker, Ines Neundorf
{"title":"Investigating the impact of thiol reactivity and disulfide formation on cellular uptake of cell-permeable peptides","authors":"Merlin Klußmann,&nbsp;Katharina Stillger,&nbsp;Melina Ruppel,&nbsp;Coco-Louisa Sticker,&nbsp;Ines Neundorf","doi":"10.1002/psc.3604","DOIUrl":"10.1002/psc.3604","url":null,"abstract":"<p>Cell-penetrating peptides (CPPs) have been explored as versatile tools to transport various molecules into cells. The uptake mechanism of CPPs is still not clearly understood and most probably depends on several factors like the nature of the CPP itself, the attached cargo, the investigated cell system, and other experimental conditions, such as temperature and concentration. One of the first steps of internalization involves the interaction of CPPs with negatively charged molecules present at the outer layer of the cell membrane. Recently, thiol-mediated uptake has been found to support the effective translocation of sulfhydryl-bearing substances that would actually not be cell-permeable. Within this work, we aimed to understand the relevance of thiol reactivity for the uptake mechanism of cysteine-containing CPPs that we have developed previously in our group. Therefore, we compared the two peptides, sC18-Cys and CaaX-1, in their single reduced and dimeric disulfide versions. Cytotoxicity, intracellular accumulation, and impact on the internalization process of the disulfides were investigated in HeLa cells. Both disulfide CPPs demonstrated significantly stronger cytotoxic effects and membrane activity compared with their reduced counterparts. Notably, thiol-mediated uptake could be excluded as a main driver for translocation, showing that peptides like CaaX-1 are most likely taken up by other mechanisms.</p>","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":null,"pages":null},"PeriodicalIF":1.8,"publicationDate":"2024-04-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/psc.3604","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140805565","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
Genetically encoded libraries and spider venoms as emerging sources for crop protective peptides 作为作物保护肽新兴来源的基因编码库和蜘蛛毒液
IF 1.8 4区 生物学
Journal of Peptide Science Pub Date : 2024-04-16 DOI: 10.1002/psc.3600
Elena Marone Fassolo, Shaodong Guo, Yachen Wang, Stefano Rosa, Volker Herzig
{"title":"Genetically encoded libraries and spider venoms as emerging sources for crop protective peptides","authors":"Elena Marone Fassolo,&nbsp;Shaodong Guo,&nbsp;Yachen Wang,&nbsp;Stefano Rosa,&nbsp;Volker Herzig","doi":"10.1002/psc.3600","DOIUrl":"10.1002/psc.3600","url":null,"abstract":"<p>Agricultural crops are targeted by various pathogens (fungi, bacteria, and viruses) and pests (herbivorous arthropods). Antimicrobial and insecticidal peptides are increasingly recognized as eco-friendly tools for crop protection due to their low propensity for resistance development and the fact that they are fully biodegradable. However, historical challenges have hindered their development, including poor stability, limited availability, reproducibility issues, high production costs, and unwanted toxicity. Toxicity is a primary concern because crop-protective peptides interact with various organisms of environmental and economic significance. This review focuses on the potential of genetically encoded peptide libraries like the use of two-hybrid-based methods for antimicrobial peptides identification and insecticidal spider venom peptides as two main approaches for targeting plant pathogens and pests. We discuss some key findings and challenges regarding the practical application of each strategy. We conclude that genetically encoded peptide library- and spider venom-derived crop protective peptides offer a sustainable and environmentally responsible approach for addressing modern crop protection needs in the agricultural sector.</p>","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":null,"pages":null},"PeriodicalIF":1.8,"publicationDate":"2024-04-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/psc.3600","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140567999","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
Design and synthesis of peptides as stabilizers of histone deacetylase 4 设计和合成多肽作为组蛋白去乙酰化酶 4 的稳定剂
IF 1.8 4区 生物学
Journal of Peptide Science Pub Date : 2024-04-16 DOI: 10.1002/psc.3603
Annika Lill, Markus Schweipert, Thomas Nehls, Eva Wurster, Frederik Lermyte, Franz-Josef Meyer-Almes, Katja Schmitz
{"title":"Design and synthesis of peptides as stabilizers of histone deacetylase 4","authors":"Annika Lill,&nbsp;Markus Schweipert,&nbsp;Thomas Nehls,&nbsp;Eva Wurster,&nbsp;Frederik Lermyte,&nbsp;Franz-Josef Meyer-Almes,&nbsp;Katja Schmitz","doi":"10.1002/psc.3603","DOIUrl":"10.1002/psc.3603","url":null,"abstract":"<p>Histone deacetylase 4 (HDAC4) contributes to gene repression by complex formation with HDAC3 and the corepressor silencing mediator for retinoid or thyroid hormone receptors (SMRT). We hypothesized that peptides derived from the class IIa specific binding site of SMRT would stabilize a specific conformation of its target protein and modulate its activity. Based on the SMRT-motif 1 (SM1) involved in the interaction of SMRT with HDAC4, we systematically developed cyclic peptides that exhibit <i>K</i><sub>i</sub> values that are 9 to 56 times lower than that of the linear SMRT peptide. The peptide macrocycles stabilize the wildtype of the catalytic domain of HDAC4 (cHDAC4) considerably better than its thermally more stable ‘gain-of-function’ (GOF) variant, cHDAC4-H976Y. Molecular docking and mutagenesis studies indicated that the cyclic peptides bind in a similar but not identical manner as the linear SMRT peptide to a discontinuous binding site. Ion mobility mass spectrometry showed no major changes in the protein fold upon peptide binding. Consistent with these results, preliminary hydrogen-deuterium exchange mass spectrometry measurements indicated only minor conformational changes. Taken together, the cyclic SMRT peptides most likely stabilize the apo form of cHDAC4.</p>","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":null,"pages":null},"PeriodicalIF":1.8,"publicationDate":"2024-04-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/psc.3603","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140567783","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
Peptide-drug conjugate designated for targeted delivery to HER2-expressing cancer cells 指定用于向表达 HER2 的癌细胞定向递送的肽药物共轭物
IF 1.8 4区 生物学
Journal of Peptide Science Pub Date : 2024-04-10 DOI: 10.1002/psc.3602
Amit Kumar Sharma, Rohit Sharma, Nitish Chauhan, Amit Das, Drishty Satpati
{"title":"Peptide-drug conjugate designated for targeted delivery to HER2-expressing cancer cells","authors":"Amit Kumar Sharma,&nbsp;Rohit Sharma,&nbsp;Nitish Chauhan,&nbsp;Amit Das,&nbsp;Drishty Satpati","doi":"10.1002/psc.3602","DOIUrl":"10.1002/psc.3602","url":null,"abstract":"<p>Targeted therapy of the highest globally incident breast cancer shall resolve the issue of off-target toxicity concurring with augmented killing of specific diseased cells. Thus, the goal of this study was to prepare a peptide-drug conjugate targeting elevated expression of HER2 receptors in breast cancer. Towards this, the rL-A9 peptide was conjugated with the chemotherapeutic drug doxorubicin (DOX) through a <i>N</i>-succinimidyl-4-(<i>N</i>-maleimidomethyl) cyclohexane-1-carboxylate (SMCC) linker. The synthesized peptide-drug conjugate, rL-A9-DOX, was characterized by mass spectrometry. Molecular docking studies, based on binding energy data, suggested a stronger interaction of rL-A9-DOX with the HER2 receptor in comparison to the unconjugated peptide, rL-A9. The cytotoxic effect of the rL-A9-DOX conjugate was observed to be higher in HER2-positive SKOV3 cells compared to HER2-negative MDA-MB-231 cells, indicating selective cell killing. Cellular internalization of the rL-A9-DOX conjugate was evident from the flow cytometry analysis, where a noticeable shift in mean fluorescent intensity (MFI) was observed for the conjugate compared to the control group. This data was further validated by confocal microscopy, where the fluorescent signal ascertained nuclear accumulation of rL-A9-DOX. The present studies highlight the promising potential of rL-A9-DOX for targeted delivery of the drug into a defined group of cancer cells.</p>","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":null,"pages":null},"PeriodicalIF":1.8,"publicationDate":"2024-04-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140568143","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
Designer tryptophan-rich peptide modulates structural dynamics of HIF-1α DNA i-motif DNA 富含色氨酸的设计肽调节 HIF-1α DNA i-motif DNA 的结构动态
IF 1.8 4区 生物学
Journal of Peptide Science Pub Date : 2024-04-09 DOI: 10.1002/psc.3601
Debasis Ghosh, Sumon Pratihar, Thimmaiah Govindaraju
{"title":"Designer tryptophan-rich peptide modulates structural dynamics of HIF-1α DNA i-motif DNA","authors":"Debasis Ghosh,&nbsp;Sumon Pratihar,&nbsp;Thimmaiah Govindaraju","doi":"10.1002/psc.3601","DOIUrl":"10.1002/psc.3601","url":null,"abstract":"<p>Cytosine-rich DNA sequences can fold into intercalated motifs known as <i>i</i>-motifs, through noncanonical hydrogen bonding interactions. Molecular probes can provide valuable insights into the conformational stability and potential cellular functions of <i>i</i>-motifs. W<sub>5</sub>K<sub>5</sub>, a decapeptide composed of alternating tryptophan (W) and lysine (K) units, has been identified as a lead candidate to modulate the structural dynamics of the hypoxia-inducible factor 1-alpha (HIF-1α) DNA <i>i</i>-motif. This finding is expected to facilitate the rational design of peptide-based probes for studying the structure and functional dynamics of <i>i</i>-motifs.</p>","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":null,"pages":null},"PeriodicalIF":1.8,"publicationDate":"2024-04-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140567780","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
Impact of glycan nature on structure and viscoelastic properties of glycopeptide hydrogels 聚糖性质对糖肽水凝胶结构和粘弹性能的影响
IF 1.8 4区 生物学
Journal of Peptide Science Pub Date : 2024-04-03 DOI: 10.1002/psc.3599
Jonas Proksch, Marlene C. S. Dal Colle, Frederick Heinz, Robert F. Schmidt, Jacqueline Gottwald, Martina Delbianco, Bettina G. Keller, Michael Gradzielski, Ulrike Alexiev, Beate Koksch
{"title":"Impact of glycan nature on structure and viscoelastic properties of glycopeptide hydrogels","authors":"Jonas Proksch,&nbsp;Marlene C. S. Dal Colle,&nbsp;Frederick Heinz,&nbsp;Robert F. Schmidt,&nbsp;Jacqueline Gottwald,&nbsp;Martina Delbianco,&nbsp;Bettina G. Keller,&nbsp;Michael Gradzielski,&nbsp;Ulrike Alexiev,&nbsp;Beate Koksch","doi":"10.1002/psc.3599","DOIUrl":"10.1002/psc.3599","url":null,"abstract":"<p>Mucus is a complex biological hydrogel that acts as a barrier for almost everything entering or exiting the body. It is therefore of emerging interest for biomedical and pharmaceutical applications. Besides water, the most abundant components are the large and densely glycosylated mucins, glycoproteins of up to 20 MDa and carbohydrate content of up to 80 wt%. Here, we designed and explored a library of glycosylated peptides to deconstruct the complexity of mucus. Using the well-characterized hFF03 coiled-coil system as a hydrogel-forming peptide scaffold, we systematically probed the contribution of single glycans to the secondary structure as well as the formation and viscoelastic properties of the resulting hydrogels. We show that glycan-decoration does not affect α-helix and coiled-coil formation while it alters gel stiffness. By using oscillatory macrorheology, dynamic light scattering microrheology, and fluorescence lifetime-based nanorheology, we characterized the glycopeptide materials over several length scales. Molecular simulations revealed that the glycosylated linker may extend into the solvent, but more frequently interacts with the peptide, thereby likely modifying the stability of the self-assembled fibers. This systematic study highlights the interplay between glycan structure and hydrogel properties and may guide the development of synthetic mucus mimetics.</p>","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":null,"pages":null},"PeriodicalIF":1.8,"publicationDate":"2024-04-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/psc.3599","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140567912","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 bright side of chemistry: Exploring synthetic peptide-based anticancer vaccines 化学的光明面探索基于合成肽的抗癌疫苗
IF 1.8 4区 生物学
Journal of Peptide Science Pub Date : 2024-04-03 DOI: 10.1002/psc.3596
Antonia D'Aniello, Alessandra Del Bene, Salvatore Mottola, Vincenzo Mazzarella, Roberto Cutolo, Erica Campagna, Salvatore Di Maro, Anna Messere
{"title":"The bright side of chemistry: Exploring synthetic peptide-based anticancer vaccines","authors":"Antonia D'Aniello,&nbsp;Alessandra Del Bene,&nbsp;Salvatore Mottola,&nbsp;Vincenzo Mazzarella,&nbsp;Roberto Cutolo,&nbsp;Erica Campagna,&nbsp;Salvatore Di Maro,&nbsp;Anna Messere","doi":"10.1002/psc.3596","DOIUrl":"10.1002/psc.3596","url":null,"abstract":"<p>The present review focuses on synthetic peptide-based vaccine strategies in the context of anticancer intervention, paying attention to critical aspects such as peptide epitope selection, adjuvant integration, and nuanced classification of synthetic peptide cancer vaccines. Within this discussion, we delve into the diverse array of synthetic peptide-based anticancer vaccines, each derived from tumor-associated antigens (TAAs), including melanoma antigen recognized by T cells 1 (Melan-A or MART-1), mucin 1 (MUC1), human epidermal growth factor receptor 2 (HER-2), tumor protein 53 (p53), human telomerase reverse transcriptase (hTERT), survivin, folate receptor (FR), cancer-testis antigen 1 (NY-ESO-1), and prostate-specific antigen (PSA). We also describe the synthetic peptide-based vaccines developed for cancers triggered by oncovirus, such as human papillomavirus (HPV), and hepatitis C virus (HCV). Additionally, the potential synergy of peptide-based vaccines with common therapeutics in cancer was considered. The last part of our discussion deals with the realm of the peptide-based vaccines delivery, highlighting its role in translating the most promising candidates into effective clinical strategies. Although this discussion does not cover all the ongoing peptide vaccine investigations, it aims at offering valuable insights into the chemical modifications and the structural complexities of anticancer peptide-based vaccines.</p>","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":null,"pages":null},"PeriodicalIF":1.8,"publicationDate":"2024-04-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140567871","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
Message 37th EPS 第 37 届 EPS.
IF 2.1 4区 生物学
Journal of Peptide Science Pub Date : 2024-03-26 DOI: 10.1002/psc.3576
{"title":"Message 37th EPS","authors":"","doi":"10.1002/psc.3576","DOIUrl":"10.1002/psc.3576","url":null,"abstract":"","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":null,"pages":null},"PeriodicalIF":2.1,"publicationDate":"2024-03-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140293854","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
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