重新设计金属肽作为定制酶模拟物的最新进展。

IF 6.9 2区 生物学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY
Salvatore La Gatta, Vincent L. Pecoraro
{"title":"重新设计金属肽作为定制酶模拟物的最新进展。","authors":"Salvatore La Gatta,&nbsp;Vincent L. Pecoraro","doi":"10.1016/j.cbpa.2025.102586","DOIUrl":null,"url":null,"abstract":"<div><div>Advances in <em>de novo</em> design of metallopeptides have paved the way for customized metalloenzyme mimics with impressive catalytic capabilities. Over the last few years, incorporation of transition metals into simplified peptide scaffolds has allowed for catalytic efficiencies similar to or greater than those found in natural metalloenzymes. Artificial <em>de novo</em> peptide scaffolds highlight how precise modifications to metal coordination environments can improve scaffold stability and catalytic efficiency for a wide range of applications towards redox, non redox, synthetic, and energy conversion chemistry. These insights deepen our understanding of enzyme evolution and set a solid foundation for new directions in biocatalysis.</div></div>","PeriodicalId":291,"journal":{"name":"Current Opinion in Chemical Biology","volume":"86 ","pages":"Article 102586"},"PeriodicalIF":6.9000,"publicationDate":"2025-03-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Recent advances in de novo designed metallopeptides as tailored enzyme mimics\",\"authors\":\"Salvatore La Gatta,&nbsp;Vincent L. Pecoraro\",\"doi\":\"10.1016/j.cbpa.2025.102586\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>Advances in <em>de novo</em> design of metallopeptides have paved the way for customized metalloenzyme mimics with impressive catalytic capabilities. Over the last few years, incorporation of transition metals into simplified peptide scaffolds has allowed for catalytic efficiencies similar to or greater than those found in natural metalloenzymes. Artificial <em>de novo</em> peptide scaffolds highlight how precise modifications to metal coordination environments can improve scaffold stability and catalytic efficiency for a wide range of applications towards redox, non redox, synthetic, and energy conversion chemistry. These insights deepen our understanding of enzyme evolution and set a solid foundation for new directions in biocatalysis.</div></div>\",\"PeriodicalId\":291,\"journal\":{\"name\":\"Current Opinion in Chemical Biology\",\"volume\":\"86 \",\"pages\":\"Article 102586\"},\"PeriodicalIF\":6.9000,\"publicationDate\":\"2025-03-20\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Current Opinion in Chemical Biology\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S1367593125000183\",\"RegionNum\":2,\"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":"Current Opinion in Chemical Biology","FirstCategoryId":"99","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S1367593125000183","RegionNum":2,"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

金属肽从头设计的进步为具有令人印象深刻的催化能力的定制金属酶模拟物铺平了道路。在过去的几年中,将过渡金属结合到简化肽支架中,使得催化效率与天然金属酶相似或更高。人工肽支架强调了对金属配位环境的精确修饰如何提高支架的稳定性和催化效率,在氧化还原、非氧化还原、合成和能量转换化学方面有着广泛的应用。这些发现加深了我们对酶进化的理解,为生物催化的新方向奠定了坚实的基础。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Recent advances in de novo designed metallopeptides as tailored enzyme mimics

Recent advances in de novo designed metallopeptides as tailored enzyme mimics
Advances in de novo design of metallopeptides have paved the way for customized metalloenzyme mimics with impressive catalytic capabilities. Over the last few years, incorporation of transition metals into simplified peptide scaffolds has allowed for catalytic efficiencies similar to or greater than those found in natural metalloenzymes. Artificial de novo peptide scaffolds highlight how precise modifications to metal coordination environments can improve scaffold stability and catalytic efficiency for a wide range of applications towards redox, non redox, synthetic, and energy conversion chemistry. These insights deepen our understanding of enzyme evolution and set a solid foundation for new directions in biocatalysis.
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
Current Opinion in Chemical Biology
Current Opinion in Chemical Biology 生物-生化与分子生物学
CiteScore
13.30
自引率
1.30%
发文量
113
审稿时长
74 days
期刊介绍: COCHBI (Current Opinion in Chemical Biology) is a systematic review journal designed to offer specialists a unique and educational platform. Its goal is to help professionals stay informed about the growing volume of information in the field of Chemical Biology through systematic reviews.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信