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Micellization and interactions with phospholipid vesicles of the lipopeptide iturin a, as monitored by time‐resolved fluorescence of a D ‐tyrosyl residue
Author(s) -
Harnois I.,
Genest D.,
Brochon J. C.,
Ptak M.
Publication year - 1988
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360270907
Subject(s) - chemistry , lipopeptide , vesicle , phospholipid , bilayer , amphiphile , fluorescence , residue (chemistry) , membrane , micelle , nanosecond , biophysics , photochemistry , organic chemistry , aqueous solution , biochemistry , bacteria , laser , optics , genetics , physics , quantum mechanics , copolymer , biology , polymer
Abstract The micellization and the interactions with lipid vesicles of the antifungal cyclic lipopeptide iturin A have been investigated by nanosecond pulse fluorometry of a D‐tyrosyl residue. We show that this lipopeptide has three conformers in solution whose proportions are modified during the micellization process. Below the critical micellar concentration (CMC) iturin A does not self‐associate inside the bilayer. Above the CMC all the molecules of iturin A interact with the vesicles and self‐associate inside the membrane.