{"title":"Peptide Stapling Using Sonogashira Coupling.","authors":"Devki Nandan, Susanta Kumar Behera, Ramesh Ramapanicker","doi":"10.1002/cbic.202500041","DOIUrl":null,"url":null,"abstract":"<p><p>An efficient method for the stapling of peptides by linking residues at the i and i+4 or i and i+7 positions through Sonagashira coupling is reported. The alkyne and aryl iodide functionality required are introduced by modifying tyrosine residues to 4-iodophenylalanine (PhI) and 4-propargyloxyphenylalanine (TyP) residues. Comparing the conformations of a stapled peptide with the corresponding linear peptide using CD spectroscopy reveals a more helical structure for the stapled peptide.</p>","PeriodicalId":140,"journal":{"name":"ChemBioChem","volume":" ","pages":"e202500041"},"PeriodicalIF":2.6000,"publicationDate":"2025-03-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"ChemBioChem","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1002/cbic.202500041","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
An efficient method for the stapling of peptides by linking residues at the i and i+4 or i and i+7 positions through Sonagashira coupling is reported. The alkyne and aryl iodide functionality required are introduced by modifying tyrosine residues to 4-iodophenylalanine (PhI) and 4-propargyloxyphenylalanine (TyP) residues. Comparing the conformations of a stapled peptide with the corresponding linear peptide using CD spectroscopy reveals a more helical structure for the stapled peptide.
期刊介绍:
ChemBioChem (Impact Factor 2018: 2.641) publishes important breakthroughs across all areas at the interface of chemistry and biology, including the fields of chemical biology, bioorganic chemistry, bioinorganic chemistry, synthetic biology, biocatalysis, bionanotechnology, and biomaterials. It is published on behalf of Chemistry Europe, an association of 16 European chemical societies, and supported by the Asian Chemical Editorial Society (ACES).