{"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 and Monika Szefczyk","doi":"10.1039/D4TB01545B","DOIUrl":null,"url":null,"abstract":"<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 <em>trans</em>-(1<em>S</em>,2<em>S</em>)-2-aminocyclopentanecarboxylic acid (<em>trans</em>-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 <em>via</em> transmission electron microscopy. The incorporation of <em>trans</em>-ACPC led to increased conformational stability and self-assembling propensity in peptides containing constrained β-amino acid residues.</p>","PeriodicalId":83,"journal":{"name":"Journal of Materials Chemistry B","volume":" 41","pages":" 10682-10691"},"PeriodicalIF":6.1000,"publicationDate":"2024-09-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.rsc.org/en/content/articlepdf/2024/tb/d4tb01545b?page=search","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 and Monika Szefczyk\",\"doi\":\"10.1039/D4TB01545B\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<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 <em>trans</em>-(1<em>S</em>,2<em>S</em>)-2-aminocyclopentanecarboxylic acid (<em>trans</em>-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 <em>via</em> transmission electron microscopy. The incorporation of <em>trans</em>-ACPC led to increased conformational stability and self-assembling propensity in peptides containing constrained β-amino acid residues.</p>\",\"PeriodicalId\":83,\"journal\":{\"name\":\"Journal of Materials Chemistry B\",\"volume\":\" 41\",\"pages\":\" 10682-10691\"},\"PeriodicalIF\":6.1000,\"publicationDate\":\"2024-09-18\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://pubs.rsc.org/en/content/articlepdf/2024/tb/d4tb01545b?page=search\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Materials Chemistry B\",\"FirstCategoryId\":\"1\",\"ListUrlMain\":\"https://pubs.rsc.org/en/content/articlelanding/2024/tb/d4tb01545b\",\"RegionNum\":3,\"RegionCategory\":\"医学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"MATERIALS SCIENCE, BIOMATERIALS\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Materials Chemistry B","FirstCategoryId":"1","ListUrlMain":"https://pubs.rsc.org/en/content/articlelanding/2024/tb/d4tb01545b","RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"MATERIALS SCIENCE, BIOMATERIALS","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.
期刊介绍：
Journal of Materials Chemistry A, B & C cover high quality studies across all fields of materials chemistry. The journals focus on those theoretical or experimental studies that report new understanding, applications, properties and synthesis of materials. Journal of Materials Chemistry A, B & C are separated by the intended application of the material studied. Broadly, applications in energy and sustainability are of interest to Journal of Materials Chemistry A, applications in biology and medicine are of interest to Journal of Materials Chemistry B, and applications in optical, magnetic and electronic devices are of interest to Journal of Materials Chemistry C.Journal of Materials Chemistry B is a Transformative Journal and Plan S compliant. Example topic areas within the scope of Journal of Materials Chemistry B are listed below. This list is neither exhaustive nor exclusive：
Antifouling coatings
Biocompatible materials
Bioelectronics
Bioimaging
Biomimetics
Biomineralisation
Bionics
Biosensors
Diagnostics
Drug delivery
Gene delivery
Immunobiology
Nanomedicine
Regenerative medicine & Tissue engineering
Scaffolds
Soft robotics
Stem cells
Therapeutic devices
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