{"title":"提高稳定性：自组装多肽结构的分层方法。","authors":"Denys Balandin, Natalia Szulc, Dominika Bystranowska, Marlena Gąsior-Głogowska, Roksana Kruszakin, Monika Szefczyk","doi":"10.1039/d4tb01545b","DOIUrl":null,"url":null,"abstract":"<p><p>The primary objective of this study was to implement a hierarchical approach to enhance the conformational stability of a selected group of peptides by incorporating <i>trans</i>-(1<i>S</i>,2<i>S</i>)-2-aminocyclopentanecarboxylic acid (<i>trans</i>-ACPC). The influence of residue mutation on the peptide structures was investigated using circular dichroism, analytical ultracentrifugation, and vibrational spectroscopy. The resulting nanostructures were examined <i>via</i> transmission electron microscopy. The incorporation of <i>trans</i>-ACPC led to increased conformational stability and self-assembling propensity in peptides containing constrained β-amino acid residues.</p>","PeriodicalId":94089,"journal":{"name":"Journal of materials chemistry. B","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2024-09-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Boosting stability: a hierarchical approach for self-assembling peptide structures.\",\"authors\":\"Denys Balandin, Natalia Szulc, Dominika Bystranowska, Marlena Gąsior-Głogowska, Roksana Kruszakin, Monika Szefczyk\",\"doi\":\"10.1039/d4tb01545b\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The primary objective of this study was to implement a hierarchical approach to enhance the conformational stability of a selected group of peptides by incorporating <i>trans</i>-(1<i>S</i>,2<i>S</i>)-2-aminocyclopentanecarboxylic acid (<i>trans</i>-ACPC). The influence of residue mutation on the peptide structures was investigated using circular dichroism, analytical ultracentrifugation, and vibrational spectroscopy. The resulting nanostructures were examined <i>via</i> transmission electron microscopy. The incorporation of <i>trans</i>-ACPC led to increased conformational stability and self-assembling propensity in peptides containing constrained β-amino acid residues.</p>\",\"PeriodicalId\":94089,\"journal\":{\"name\":\"Journal of materials chemistry. B\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2024-09-24\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of materials chemistry. B\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1039/d4tb01545b\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of materials chemistry. B","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1039/d4tb01545b","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Boosting stability: a hierarchical approach for self-assembling peptide structures.
The primary objective of this study was to implement a hierarchical approach to enhance the conformational stability of a selected group of peptides by incorporating trans-(1S,2S)-2-aminocyclopentanecarboxylic acid (trans-ACPC). The influence of residue mutation on the peptide structures was investigated using circular dichroism, analytical ultracentrifugation, and vibrational spectroscopy. The resulting nanostructures were examined via transmission electron microscopy. The incorporation of trans-ACPC led to increased conformational stability and self-assembling propensity in peptides containing constrained β-amino acid residues.
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