Structure-activity relationships in the peptide antibiotic nisin: antibacterial activity of fragments of nisin.
FEBS Lett
; 390(2): 129-32, 1996 Jul 22.
Article
em En
| MEDLINE
| ID: mdl-8706842
ABSTRACT
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 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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fragmentos de Peptídeos
/
Peptídeos
/
Proteínas de Bactérias
/
Antibacterianos
/
Nisina
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
1996
Tipo de documento:
Article
País de afiliação:
Reino Unido