优化基于肽折叠聚合物的人工逆醛酸酶

IF 4.4 3区化学 Q2 CHEMISTRY, PHYSICAL

Catalysis Science & Technology Pub Date : 2024-08-12 DOI:10.1039/d4cy00342j

Katarzyna Ożga , Ewa Rudzińska-Szostak , Łukasz Berlicki

{"title":"优化基于肽折叠聚合物的人工逆醛酸酶","authors":"Katarzyna Ożga , Ewa Rudzińska-Szostak , Łukasz Berlicki","doi":"10.1039/d4cy00342j","DOIUrl":null,"url":null,"abstract":"<div><p>Due to their predictable and controllable three-dimensional structure, peptide foldamers constitute a class of compounds beneficial for developing functional molecules. One of the most challenging applications is the construction of enzyme-like catalysts. Here, we describe the optimization of peptide foldamers composed of two 9/12/9/10-helices incorporating <em>cis</em>-2-aminocyclopentanecarboxylic acid residues toward retro-aldol activity. Modifications related to helix handedness, interhelical linker rigidity, and active site construction led to highly active retro-aldolase mimetics. NMR measurements confirmed the assumed arrangement of active site residues.</p></div>","PeriodicalId":66,"journal":{"name":"Catalysis Science & Technology","volume":"14 16","pages":"Pages 4533-4541"},"PeriodicalIF":4.4000,"publicationDate":"2024-08-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Optimization of peptide foldamer-based artificial retro-aldolase†\",\"authors\":\"Katarzyna Ożga , Ewa Rudzińska-Szostak , Łukasz Berlicki\",\"doi\":\"10.1039/d4cy00342j\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Due to their predictable and controllable three-dimensional structure, peptide foldamers constitute a class of compounds beneficial for developing functional molecules. One of the most challenging applications is the construction of enzyme-like catalysts. Here, we describe the optimization of peptide foldamers composed of two 9/12/9/10-helices incorporating <em>cis</em>-2-aminocyclopentanecarboxylic acid residues toward retro-aldol activity. Modifications related to helix handedness, interhelical linker rigidity, and active site construction led to highly active retro-aldolase mimetics. NMR measurements confirmed the assumed arrangement of active site residues.</p></div>\",\"PeriodicalId\":66,\"journal\":{\"name\":\"Catalysis Science & Technology\",\"volume\":\"14 16\",\"pages\":\"Pages 4533-4541\"},\"PeriodicalIF\":4.4000,\"publicationDate\":\"2024-08-12\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Catalysis Science & Technology\",\"FirstCategoryId\":\"92\",\"ListUrlMain\":\"https://www.sciencedirect.com/org/science/article/pii/S2044475324003927\",\"RegionNum\":3,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"CHEMISTRY, PHYSICAL\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Catalysis Science & Technology","FirstCategoryId":"92","ListUrlMain":"https://www.sciencedirect.com/org/science/article/pii/S2044475324003927","RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"CHEMISTRY, PHYSICAL","Score":null,"Total":0}

引用次数: 0

摘要

肽折叠体具有可预测和可控制的三维结构，是一类有利于开发功能分子的化合物。其中最具挑战性的应用之一是构建类似酶的催化剂。在这里，我们介绍了如何优化由两个 9/12/9/10 螺旋组成的多肽折叠体，使其具有顺式-2-氨基环戊烷羧酸残基的逆醛醇活性。通过对螺旋手性、螺旋间连接刚性和活性位点结构的修改，产生了高活性的逆醛酸酶模拟物。核磁共振测量证实了活性位点残基的假定排列。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

Optimization of peptide foldamer-based artificial retro-aldolase†

查看原文本刊更多论文

Optimization of peptide foldamer-based artificial retro-aldolase†

Due to their predictable and controllable three-dimensional structure, peptide foldamers constitute a class of compounds beneficial for developing functional molecules. One of the most challenging applications is the construction of enzyme-like catalysts. Here, we describe the optimization of peptide foldamers composed of two 9/12/9/10-helices incorporating cis-2-aminocyclopentanecarboxylic acid residues toward retro-aldol activity. Modifications related to helix handedness, interhelical linker rigidity, and active site construction led to highly active retro-aldolase mimetics. NMR measurements confirmed the assumed arrangement of active site residues.

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

Catalysis Science & Technology CHEMISTRY, PHYSICAL-

CiteScore

8.70

自引率

6.00%

发文量

587

审稿时长

1.5 months

期刊介绍： A multidisciplinary journal focusing on cutting edge research across all fundamental science and technological aspects of catalysis. Editor-in-chief: Bert Weckhuysen Impact factor: 5.0 Time to first decision (peer reviewed only): 31 days