Structure-activity relationships in the peptide antibiotic nisin: Antibacterial activity of fragments of nisin

W. C. Chan, M. Leyland, J. Clark, H. M. Dodd, L. Y. Lian, M. J. Gasson, B. W. Bycroft, G. C K Roberts

    Research output: Contribution to journalArticlepeer-review


    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 same differences between analogous fragments of nisin and subtilin, suggesting possible subtle differences in made of action. Cleavage within, or removal of, lanthionine ring C essentially abolishes the activity of nisin. The fragment nisin1-12 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.
    Original languageEnglish
    Pages (from-to)129-132
    Number of pages3
    JournalFEBS Letters
    Issue number2
    Publication statusPublished - 22 Jul 1996


    • Lantibiotic
    • Nisin
    • Peptide antibiotic
    • Proteolysis
    • Structure-activity relationships


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