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Article

Surface location and orientation of the lantibiotic nisin bound to membrane-mimicking micelles of dodecylphosphocholine and of sodium dodecylsulphate.

European journal of biochemistry - 15 Jan 1996

Van Den Hooven H W, Spronk C A, Van De Kamp M, Konings R N, Hilbers C W, Van De Van F J

Abstract excerpt

The interaction of nisin, a membrane-interacting cationic polypeptide, with membrane-mimicking micelles of zwitterionic dodecylphosphocholine and of anionic sodium dodecylsulphate was studied. Direct contacts have been established through the observation of NOEs between nisin and micelle protons. Spin-labeled DOXYL-stearic acids were incorporated into the two micellar systems. From the paramagnetic broadening...

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PMID: 8631359
DOI: 10.1111/j.1432-1033.1996.00394.x

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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