Journal of Peptide Science最新文献_第6页

The European Peptide Society Newsletter 欧洲多肽学会通讯

IF 2.1 4区生物学

Journal of Peptide Science Pub Date : 2024-03-26 DOI: 10.1002/psc.3574

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10th International Meeting on Antimicrobial Peptides (IMAP) 第 10 届国际抗菌肽会议（IMAP）

IF 2.1 4区生物学

Journal of Peptide Science Pub Date : 2024-03-26 DOI: 10.1002/psc.3580

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Peptide Chemistry Day symposium 多肽化学日研讨会。

IF 2.1 4区生物学

Journal of Peptide Science Pub Date : 2024-03-26 DOI: 10.1002/psc.3582

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Extract from the Minutes of the EC Meeting, 22 and 23 of March 2023 (Videoconference) 2023 年 3 月 22 日和 23 日执委会会议（视频会议）记录摘录

IF 2.1 4区生物学

Journal of Peptide Science Pub Date : 2024-03-26 DOI: 10.1002/psc.3587

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Society Officers 协会官员

IF 2.1 4区生物学

Journal of Peptide Science Pub Date : 2024-03-26 DOI: 10.1002/psc.3590

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Bergofungin D, a peptaibol template for the introduction of chemical modifications, synthesis of analogs and comparative studies of their structures Bergofungin D，一种用于引入化学修饰、合成类似物并对其结构进行比较研究的 peptaibol 模板。

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2024-03-26 DOI: 10.1002/psc.3598

Sanjit Das, Khoubaib Haj Ben Salah, Emmanuel Wenger, Baptiste Legrand, Claude Didierjean, Nicolas Inguimbert

{"title":"Bergofungin D, a peptaibol template for the introduction of chemical modifications, synthesis of analogs and comparative studies of their structures","authors":"Sanjit Das, Khoubaib Haj Ben Salah, Emmanuel Wenger, Baptiste Legrand, Claude Didierjean, Nicolas Inguimbert","doi":"10.1002/psc.3598","DOIUrl":"10.1002/psc.3598","url":null,"abstract":"Bergofungin D is a helical peptide of the peptaibol family consisting of 14 amino acids, six of which are the helix inducer aminoisobutyric acid (Aib). In the second third of the sequence, a hydroxyproline causes a bending of the helix and a disruption of the hydrogen bond network, and Aib7 is the only amino acid in this region involved in the hydrogen bond network. Therefore, modification of this residue can serve as a probe to monitor the effect of introducing amino acid substitutions on this more fragile helical turn. To validate this approach, we simplified the original bergofungin D by reducing the number of non-classical amino acids, replacing the (R)-isovaleric acid by its enantiomer or an Aib and the hydroxyproline with a proline, respectively, without affecting its secondary structure. Within the modified structure, we replaced Aib7-Aib8 by its 1,2,3-triazolodipeptide equivalent or Aib7 by a serine or a dehydrobutyrine. We have reported and analyzed five crystal structures, three of which are new, demonstrating the usefulness of the modified bergofungin D as a probe for monitoring the introduction of amino acid substitutions within a helical structure.","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":null,"pages":null},"PeriodicalIF":1.8,"publicationDate":"2024-03-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140293850","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

N-terminal modification of an LAH4-derived peptide increases mRNA delivery in the presence of serum 在血清存在的情况下，对 LAH4 衍生肽进行 N 端修饰可增加 mRNA 的传递。

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2024-03-25 DOI: 10.1002/psc.3597

Candice Dussouillez, Morane Lointier, Mohammed-Karim Sebane, Sylvie Fournel, Burkhard Bechinger, Antoine Kichler

引用次数: 0

Supercharged coiled-coil protein with N-terminal decahistidine tag boosts siRNA complexation and delivery efficiency of a lipoproteoplex 带有 N 端癸脒标签的增压盘绕蛋白提高了脂蛋白复合物的 siRNA 复合物和递送效率。

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2024-03-18 DOI: 10.1002/psc.3594

Jonathan W. Sun, Joseph S. Thomas, Julia M. Monkovic, Halle Gibson, Akash Nagapurkar, Joseph A. Frezzo, Priya Katyal, Kamia Punia, Farbod Mahmoudinobar, P. Douglas Renfrew, Jin Kim Montclare

{"title":"Supercharged coiled-coil protein with N-terminal decahistidine tag boosts siRNA complexation and delivery efficiency of a lipoproteoplex","authors":"Jonathan W. Sun, Joseph S. Thomas, Julia M. Monkovic, Halle Gibson, Akash Nagapurkar, Joseph A. Frezzo, Priya Katyal, Kamia Punia, Farbod Mahmoudinobar, P. Douglas Renfrew, Jin Kim Montclare","doi":"10.1002/psc.3594","DOIUrl":"10.1002/psc.3594","url":null,"abstract":"Short interfering RNA (siRNA) therapeutics have soared in popularity due to their highly selective and potent targeting of faulty genes, providing a non-palliative approach to address diseases. Despite their potential, effective transfection of siRNA into cells requires the assistance of an accompanying vector. Vectors constructed from non-viral materials, while offering safer and non-cytotoxic profiles, often grapple with lackluster loading and delivery efficiencies, necessitating substantial milligram quantities of expensive siRNA to confer the desired downstream effects. We detail the recombinant synthesis of a diverse series of coiled-coil supercharged protein (CSP) biomaterials systematically designed to investigate the impact of two arginine point mutations (Q39R and N61R) and decahistidine tags on liposomal siRNA delivery. The most efficacious variant, N8, exhibits a twofold increase in its affinity to siRNA and achieves a twofold enhancement in transfection activity with minimal cytotoxicity in vitro. Subsequent analysis unveils the destabilizing effect of the Q39R and N61R supercharging mutations and the incorporation of C-terminal decahistidine tags on α-helical secondary structure. Cross-correlational regression analyses reveal that the amount of helical character in these mutants is key in N8's enhanced siRNA complexation and downstream delivery efficiency.","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":null,"pages":null},"PeriodicalIF":1.8,"publicationDate":"2024-03-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140158379","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

Wound microenvironment-responsive peptide hydrogel with multifunctionalities for accelerating wound healing 具有多功能性的伤口微环境响应肽水凝胶，可加速伤口愈合。

IF 2.1 4区生物学

Journal of Peptide Science Pub Date : 2024-03-17 DOI: 10.1002/psc.3595

Weimiao Dong, Haihong Yang, Min Liu, Leixia Mei, Jun Han

{"title":"Wound microenvironment-responsive peptide hydrogel with multifunctionalities for accelerating wound healing","authors":"Weimiao Dong, Haihong Yang, Min Liu, Leixia Mei, Jun Han","doi":"10.1002/psc.3595","DOIUrl":"10.1002/psc.3595","url":null,"abstract":"The fabrication of wound microenvironment-responsive peptide hydrogels with hemostatic ability, antibacterial activity, and wound healing potential remains a challenge. Herein, we constructed a multifunctional dressing by inducing the self-assembly of a peptide (Pep-1) and water-soluble new methylene blue (NMB) through electrostatic interaction. The self-assembly mechanism was demonstrated using a combination of transmission electron microscopy, circular dichroism spectrum, fluorescence spectrum, Zeta potential, and rheological analysis. The Pep-1/NMB hydrogel also exhibited a faster drug release rate in wound acidic environment. Furthermore, when Pep-1/NMB was exposed to a 635 nm laser, its antibacterial ratios increased sharply to 95.3%, indicating remarkably improved antibacterial effects. The findings from the blood coagulation and hemostasis assay indicated that Pep-1/NMB effectively enhanced the speed of blood clotting in vitro and efficiently controlled hemorrhage in a mouse liver hemorrhage model. Meanwhile, hemolytic and cytotoxicity evaluation revealed that the hydrogel had excellent hemocompatibility and cytocompatibility. Finally, the findings from the wound healing studies and H&E staining indicated that the Pep-1/NMB hydrogel had a significant impact on cell migration and wound repair. The results indicated that wound microenvironment-responsive Pep-1/NMB hydrogel had significant potential as a highly effective wound dressing platform, offering rapid hemostasis, antibacterial, and wound healing acceleration properties.","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":null,"pages":null},"PeriodicalIF":2.1,"publicationDate":"2024-03-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140143664","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

Hybrid peptide-PNA monomers as building blocks for the fabrication of supramolecular aggregates 混合肽-PNA 单体作为制造超分子聚合体的构件。

IF 2.1 4区生物学

Journal of Peptide Science Pub Date : 2024-03-12 DOI: 10.1002/psc.3573

Luca Cimmino, Carlo Diaferia, Mariangela Rosa, Giancarlo Morelli, Elisabetta Rosa, Antonella Accardo

{"title":"Hybrid peptide-PNA monomers as building blocks for the fabrication of supramolecular aggregates","authors":"Luca Cimmino, Carlo Diaferia, Mariangela Rosa, Giancarlo Morelli, Elisabetta Rosa, Antonella Accardo","doi":"10.1002/psc.3573","DOIUrl":"10.1002/psc.3573","url":null,"abstract":"Advantages like biocompatibility, biodegradability and tunability allowed the exploitation of peptides and peptidomimetics as versatile therapeutic or diagnostic agents. Because of their selectivity towards transmembrane receptors or cell membranes, peptides have also been identified as suitable molecules able to deliver in vivo macromolecules, proteins or nucleic acids. However, after the identification of the homodimer diphenylalanine (FF) as an aggregative motif inside the Aβ1–42 polypeptide, short and ultrashort peptides have been studied as building blocks for the fabrication of supramolecular, ordered nanostructures for applications in biotechnological, biomedical and industrial fields. In this perspective, many hybrid molecules that combine FF with other chemical entities have been synthesized and characterized. Two novel hybrid derivatives (tFaF and cFgF), in which the FF homodimer is alternated with the peptide-nucleic acid (PNA) heterodimer “g-c” (guanine-cytosine) or “a-t” (adenine-thymine) and their dimeric forms (tFaF)2 and (cFgF)2 were synthesized. The structural characterization performed by circular dichroism (CD), Fourier transform infrared (FTIR) and fluorescence spectroscopies highlighted the capability of all the FF-PNA derivatives to self-assemble into β-sheet structures. As a consequence of this supramolecular organization, the resulting aggregates also exhibit optoelectronic properties already reported for other similar nanostructures. This photoemissive behavior is promising for their potential applications in bioimaging.","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":null,"pages":null},"PeriodicalIF":2.1,"publicationDate":"2024-03-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140110456","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