✦ LIBER ✦
Micellization and interactions with phospholipid vesicles of the lipopeptide iturin a, as monitored by time-resolved fluorescence of a D-tyrosyl residue
✍ Scribed by I. Harnois; D. Genest; J. C. Brochon; M. Ptak
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1988
- Tongue
- English
- Weight
- 642 KB
- Volume
- 27
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
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.