{"title":"一种新的抗生素耐药机制:多肽与金黄色葡萄球菌核糖体复合物状态的研究","authors":"Laurent Verdier , Josyane Gharbi-Benarous , Gildas Bertho , Pascale Mauvais , Jean-Pierre Girault","doi":"10.1016/S1387-1609(01)01316-0","DOIUrl":null,"url":null,"abstract":"<div><p>Two antibiotic resistance peptides, the E-peptide (MRLFV) and the K-peptide (MRFFV) conferring macrolide and ketolide resistance, respectively, were studied in the complex state with bacterial <em>Staphylococcus aureus</em> ribosomes after a conformational analysis by NMR spectroscopy and molecular modeling of the unbound molecules. <em>T</em>2 (CPMG) measurements were used to characterize equilibrium binding of antibiotic resistance peptides to bacterial ribosomes. Additionally, interactions of antibiotic resistance peptide to ribosomes were investigated using two-dimensional transferred nuclear Overhauser effect spectroscopy (TRNOESY), resulting in bound structures compatible with the experimental NMR data.</p></div>","PeriodicalId":100305,"journal":{"name":"Comptes Rendus de l'Académie des Sciences - Series IIC - Chemistry","volume":"4 10","pages":"Pages 745-750"},"PeriodicalIF":0.0000,"publicationDate":"2001-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S1387-1609(01)01316-0","citationCount":"1","resultStr":"{\"title\":\"A novel mechanism of antibiotic resistance: study of the complex state of peptides with bacterial Staphylococcus aureus ribosomes\",\"authors\":\"Laurent Verdier , Josyane Gharbi-Benarous , Gildas Bertho , Pascale Mauvais , Jean-Pierre Girault\",\"doi\":\"10.1016/S1387-1609(01)01316-0\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Two antibiotic resistance peptides, the E-peptide (MRLFV) and the K-peptide (MRFFV) conferring macrolide and ketolide resistance, respectively, were studied in the complex state with bacterial <em>Staphylococcus aureus</em> ribosomes after a conformational analysis by NMR spectroscopy and molecular modeling of the unbound molecules. <em>T</em>2 (CPMG) measurements were used to characterize equilibrium binding of antibiotic resistance peptides to bacterial ribosomes. Additionally, interactions of antibiotic resistance peptide to ribosomes were investigated using two-dimensional transferred nuclear Overhauser effect spectroscopy (TRNOESY), resulting in bound structures compatible with the experimental NMR data.</p></div>\",\"PeriodicalId\":100305,\"journal\":{\"name\":\"Comptes Rendus de l'Académie des Sciences - Series IIC - Chemistry\",\"volume\":\"4 10\",\"pages\":\"Pages 745-750\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2001-10-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/S1387-1609(01)01316-0\",\"citationCount\":\"1\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Comptes Rendus de l'Académie des Sciences - Series IIC - Chemistry\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S1387160901013160\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Comptes Rendus de l'Académie des Sciences - Series IIC - Chemistry","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S1387160901013160","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
A novel mechanism of antibiotic resistance: study of the complex state of peptides with bacterial Staphylococcus aureus ribosomes
Two antibiotic resistance peptides, the E-peptide (MRLFV) and the K-peptide (MRFFV) conferring macrolide and ketolide resistance, respectively, were studied in the complex state with bacterial Staphylococcus aureus ribosomes after a conformational analysis by NMR spectroscopy and molecular modeling of the unbound molecules. T2 (CPMG) measurements were used to characterize equilibrium binding of antibiotic resistance peptides to bacterial ribosomes. Additionally, interactions of antibiotic resistance peptide to ribosomes were investigated using two-dimensional transferred nuclear Overhauser effect spectroscopy (TRNOESY), resulting in bound structures compatible with the experimental NMR data.
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