{"title":"合成多肽作为结合步骤的催化模拟物。","authors":"E Pérez-Payá, R A Houghten, S E Blondelle","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Peptides able to adopt an environment-dependent secondary structure represent attractive models for enzyme mimics. An approach to design new synthetic enzyme-like peptides involves the use of binding-step based mimics. The polypeptide melittin, based on its intrinsic ability to bind to phospholipids, was selected as a potential binding-step based catalytic mimic. Synthetic melittin was found to exhibit weak but reproducible phospholipase-like activity. The rate enhancement of the hydrolysis of phospholipids, although far from that of the natural enzyme, was encouraging as a first step in the development of new catalytic peptides.</p>","PeriodicalId":20005,"journal":{"name":"Peptide research","volume":"7 6","pages":"286-8"},"PeriodicalIF":0.0000,"publicationDate":"1994-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Synthetic peptides as binding-step based catalytic mimics.\",\"authors\":\"E Pérez-Payá, R A Houghten, S E Blondelle\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Peptides able to adopt an environment-dependent secondary structure represent attractive models for enzyme mimics. An approach to design new synthetic enzyme-like peptides involves the use of binding-step based mimics. The polypeptide melittin, based on its intrinsic ability to bind to phospholipids, was selected as a potential binding-step based catalytic mimic. Synthetic melittin was found to exhibit weak but reproducible phospholipase-like activity. The rate enhancement of the hydrolysis of phospholipids, although far from that of the natural enzyme, was encouraging as a first step in the development of new catalytic peptides.</p>\",\"PeriodicalId\":20005,\"journal\":{\"name\":\"Peptide research\",\"volume\":\"7 6\",\"pages\":\"286-8\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1994-11-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Peptide research\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Peptide research","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Synthetic peptides as binding-step based catalytic mimics.
Peptides able to adopt an environment-dependent secondary structure represent attractive models for enzyme mimics. An approach to design new synthetic enzyme-like peptides involves the use of binding-step based mimics. The polypeptide melittin, based on its intrinsic ability to bind to phospholipids, was selected as a potential binding-step based catalytic mimic. Synthetic melittin was found to exhibit weak but reproducible phospholipase-like activity. The rate enhancement of the hydrolysis of phospholipids, although far from that of the natural enzyme, was encouraging as a first step in the development of new catalytic peptides.