Shubhasree Das , Rongali G. Sravani , Shibaji Basak
{"title":"合成核肽和核苷酸的动力学捕获自组装","authors":"Shubhasree Das , Rongali G. Sravani , Shibaji Basak","doi":"10.1039/d4cc06524g","DOIUrl":null,"url":null,"abstract":"<div><div>Nature uses thermodynamically unfavourable dynamic self-assembly to execute cellular functions frequently. A nucleopeptide and ATP formed a self-assembled hydrogel. The peptide and AMP were unable to form a hydrogel. Notably, when ATP was hydrolyzed to AMP <em>in situ</em> by an ATPase enzyme, the peptide–AMP composition remained a self-assembled hydrogel, showing unusual kinetically trapped self-assembly.</div></div>","PeriodicalId":67,"journal":{"name":"Chemical Communications","volume":"61 31","pages":"Pages 5802-5805"},"PeriodicalIF":4.2000,"publicationDate":"2025-03-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Kinetically trapped self-assembly in synthetic nucleopeptides and nucleotides†\",\"authors\":\"Shubhasree Das , Rongali G. Sravani , Shibaji Basak\",\"doi\":\"10.1039/d4cc06524g\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>Nature uses thermodynamically unfavourable dynamic self-assembly to execute cellular functions frequently. A nucleopeptide and ATP formed a self-assembled hydrogel. The peptide and AMP were unable to form a hydrogel. Notably, when ATP was hydrolyzed to AMP <em>in situ</em> by an ATPase enzyme, the peptide–AMP composition remained a self-assembled hydrogel, showing unusual kinetically trapped self-assembly.</div></div>\",\"PeriodicalId\":67,\"journal\":{\"name\":\"Chemical Communications\",\"volume\":\"61 31\",\"pages\":\"Pages 5802-5805\"},\"PeriodicalIF\":4.2000,\"publicationDate\":\"2025-03-14\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Chemical Communications\",\"FirstCategoryId\":\"92\",\"ListUrlMain\":\"https://www.sciencedirect.com/org/science/article/pii/S1359734525005567\",\"RegionNum\":2,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"CHEMISTRY, MULTIDISCIPLINARY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Chemical Communications","FirstCategoryId":"92","ListUrlMain":"https://www.sciencedirect.com/org/science/article/pii/S1359734525005567","RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"CHEMISTRY, MULTIDISCIPLINARY","Score":null,"Total":0}
Kinetically trapped self-assembly in synthetic nucleopeptides and nucleotides†
Nature uses thermodynamically unfavourable dynamic self-assembly to execute cellular functions frequently. A nucleopeptide and ATP formed a self-assembled hydrogel. The peptide and AMP were unable to form a hydrogel. Notably, when ATP was hydrolyzed to AMP in situ by an ATPase enzyme, the peptide–AMP composition remained a self-assembled hydrogel, showing unusual kinetically trapped self-assembly.
期刊介绍:
ChemComm (Chemical Communications) is renowned as the fastest publisher of articles providing information on new avenues of research, drawn from all the world''s major areas of chemical research.