The lantibiotic nisin induces transmembrane movement of a fluorescent phospholipid.

Abstract:

:Nisin is a pore-forming antimicrobial peptide. The capacity of nisin to induce transmembrane movement of a fluorescent phospholipid in lipid vesicles was investigated. Unilamellar phospholipid vesicles that contained a fluorescent phospholipid (1-acyl-2-(6-[(7-nitro-2-1, 3-benzoxadiazol-4-yl)amino]caproyl)-sn-glycero-3-phosphocholine) in the inner leaflet of the bilayer were used. Nisin-induced movement of the fluorescent phospholipid from the inner leaflet to the outer leaflet of the membrane reached stable levels, which were dependent on the concentration of nisin added. The rate constant k of this nisin-induced transmembrane movement increased with the nisin concentration but was not dependent on temperature within the range of 5 to 30 degrees C. In contrast, the rate constant of movement of fluorescent phospholipid from vesicle to vesicle strongly depended on temperature. The data indicate that nisin transiently disturbs the phospholipid organization of the target membrane.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Moll GN,Konings WN,Driessen AJ

doi

10.1128/JB.180.24.6565-6570.1998

subject

Has Abstract

pub_date

1998-12-01 00:00:00

pages

6565-70

issue

24

eissn

0021-9193

issn

1098-5530

journal_volume

180

pub_type

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