{"title":"Optimization of peptide foldamer-based artificial retro-aldolase†","authors":"","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":null,"pages":null},"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}
引用次数: 0
Abstract
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.
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