连续筛选大肠杆菌中环状肽蛋白聚集抑制剂的鉴定

IF 12.9 1区生物学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY

Nature chemical biology Pub Date : 2025-01-17 DOI:10.1038/s41589-024-01824-w

{"title":"连续筛选大肠杆菌中环状肽蛋白聚集抑制剂的鉴定","authors":"","doi":"10.1038/s41589-024-01824-w","DOIUrl":null,"url":null,"abstract":"Targeting of protein aggregates is technologically challenging. We developed a phage-assisted continuous evolution platform for rapid selection of protein aggregation inhibitors from genetically encoded cyclic peptide libraries in Escherichia coli. This strategy enabled discovery of cyclic peptides that suppress the aggregation of two clinically relevant proteins, amyloid-β42 (Aβ42) and human islet amyloid polypeptide (hIAPP).","PeriodicalId":18832,"journal":{"name":"Nature chemical biology","volume":"37 1","pages":""},"PeriodicalIF":12.9000,"publicationDate":"2025-01-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Continuous selection in E. coli to identify cyclic peptide inhibitors of protein aggregation\",\"authors\":\"\",\"doi\":\"10.1038/s41589-024-01824-w\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Targeting of protein aggregates is technologically challenging. We developed a phage-assisted continuous evolution platform for rapid selection of protein aggregation inhibitors from genetically encoded cyclic peptide libraries in Escherichia coli. This strategy enabled discovery of cyclic peptides that suppress the aggregation of two clinically relevant proteins, amyloid-β42 (Aβ42) and human islet amyloid polypeptide (hIAPP).\",\"PeriodicalId\":18832,\"journal\":{\"name\":\"Nature chemical biology\",\"volume\":\"37 1\",\"pages\":\"\"},\"PeriodicalIF\":12.9000,\"publicationDate\":\"2025-01-17\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Nature chemical biology\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1038/s41589-024-01824-w\",\"RegionNum\":1,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Nature chemical biology","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1038/s41589-024-01824-w","RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}

引用次数: 0

摘要

靶向蛋白质聚集体在技术上具有挑战性。我们开发了一个噬菌体辅助的连续进化平台，用于从大肠杆菌的遗传编码环肽文库中快速选择蛋白质聚集抑制剂。这一策略使得环状肽能够抑制两种临床相关蛋白的聚集，即淀粉样蛋白-β42 （Aβ42）和人胰岛淀粉样蛋白多肽（hIAPP）。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

Continuous selection in E. coli to identify cyclic peptide inhibitors of protein aggregation

查看原文本刊更多论文

Continuous selection in E. coli to identify cyclic peptide inhibitors of protein aggregation

Targeting of protein aggregates is technologically challenging. We developed a phage-assisted continuous evolution platform for rapid selection of protein aggregation inhibitors from genetically encoded cyclic peptide libraries in Escherichia coli. This strategy enabled discovery of cyclic peptides that suppress the aggregation of two clinically relevant proteins, amyloid-β42 (Aβ42) and human islet amyloid polypeptide (hIAPP).

求助全文

通过发布文献求助，成功后即可免费获取论文全文。去求助

来源期刊

Nature chemical biology 生物-生化与分子生物学

CiteScore

23.90

自引率

1.40%

发文量

238

审稿时长

12 months

期刊介绍： Nature Chemical Biology stands as an esteemed international monthly journal, offering a prominent platform for the chemical biology community to showcase top-tier original research and commentary. Operating at the crossroads of chemistry, biology, and related disciplines, chemical biology utilizes scientific ideas and approaches to comprehend and manipulate biological systems with molecular precision. The journal embraces contributions from the growing community of chemical biologists, encompassing insights from chemists applying principles and tools to biological inquiries and biologists striving to comprehend and control molecular-level biological processes. We prioritize studies unveiling significant conceptual or practical advancements in areas where chemistry and biology intersect, emphasizing basic research, especially those reporting novel chemical or biological tools and offering profound molecular-level insights into underlying biological mechanisms. Nature Chemical Biology also welcomes manuscripts describing applied molecular studies at the chemistry-biology interface due to the broad utility of chemical biology approaches in manipulating or engineering biological systems. Irrespective of scientific focus, we actively seek submissions that creatively blend chemistry and biology, particularly those providing substantial conceptual or methodological breakthroughs with the potential to open innovative research avenues. The journal maintains a robust and impartial review process, emphasizing thorough chemical and biological characterization.