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Structure‐activity relationships in the peptide antibiotic nisin: antibacterial activity of fragments of nisin
Author(s) -
Chan W.C.,
Leyland M.,
Clark J.,
Dodd H.M.,
Lian L.-Y.,
Gasson M.J.,
Bycroft B.W.,
Roberts G.C.K.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00638-2
Subject(s) - nisin , lanthionine , lantibiotics , micrococcus luteus , lactococcus lactis , bacteriocin , lipid ii , peptide , biochemistry , chemistry , virginiamycin , antibacterial agent , bacteria , antibiotics , microbiology and biotechnology , biology , antimicrobial , biosynthesis , escherichia coli , enzyme , lactic acid , genetics , gene
The post‐translationally modified peptide antibiotic nisin has been cleaved by a number of proteases and the fragments produced purified, characterised chemically, and assayed for activity in inhibiting the growth of Lactococcus lactis MG1614 and Micrococcus luteus NCDO8166. These results provide information on the importance of different parts of the nisin molecule for its growth‐inhibition activity. Removal of the C‐terminal five residues leads to approximately a 10‐fold decrease in potency, while removal of a further nine residues, encompassing two of the lanthionine rings, leads to a 100‐fold decrease. There are some differences between analogous fragments of nisin and subtilin, suggesting possible subtle differences in mode of action. Cleavage within, or removal of, lanthionine ring C essentially abolishes the activity of nisin. The fragment nisin 1−12 is inactive itself, and specifically antagonises the growth‐inhibitory action of nisin. These results are discussed in terms of current models for the mechanism of action of nisin.