Isolation and characterisation of two degradation products derived from the peptide antibiotic nisin

FEBS Letters

Chan, Weng C.²  Bycroft, Barrie W.²  Lian, Lu-Yun¹  Roberts, Gordon C.K.¹ 

[1]Biological NMR Centre, University of Leicester, Leicester LE1 9HN, England

[2]Department of Pharmaceutical Sciences, University of Nottingham, Nottingham NG7 2RD England

关键词: Nisin;    Peptide antibiotic;    HPLC;    NMR;    Peptide structure;    HPLC;    high pressure liquid chromatography;    2D NMR;    two-dimensional nuclear magnetic resonance;    HOHAHA;    homonuclear Hartmann-Hahn experiment;    NOESY;    nuclear Overhauser enhancement spectroscopy;   

DOI  :  10.1016/0014-5793(89)80884-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Two degradation products of nisin have been isolated and their structures have been determined by ¹H NMR. Nisin^1–32 [(des-ΔAla33-Lys34; Val32-NH₂)nisin] and (des-ΔAla5)nisin^1–32 [(des-ΔAla5, ΔAla33-Lys34; Ile4-NH₂, pyruvyl-Leu6, Val32-NH₂)nisin] are formed on storage or by acid treatment. Contrary to previous reports, nisin^1–32 showed potent antimicrobial activity against Gram-positive organisms comparable to that of nisin itself. (des-ΔAla5)Nisin^1–32, however, was biologically inactive, thus demonstrating the importance of ΔAla5 and/or ring A for biological activity.

【 授权许可】

Unknown