Micellization and interactions with phospholipid vesicles of the lipopeptide iturin a, as monitored by time‐resolved fluorescence of a  D ‐tyrosyl residue | Zendy

Harnois I. | Zendy; Genest D. | Zendy; Brochon J. C. | Zendy; Ptak M. | Zendy

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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

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.

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