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An amphipathic class A peptide, Ac-18A-NH2, has been employed in modeling the -helical lipid-binding site of apolipoprotein A-I (apoA-I). To gain insight into the nature of proteinlipid interactions responsible for the ability of apoA-I to promote the efflux of intracellular cholesterol, the peptide disposition in model membranes composed of phosphatidylcholine (PC) and its mixture with cholesterol...
Resonance energy transfer involving tryptophan as a donor and anthrylvinyl-labeled phosphatidylcholine (AV-PC), 3-methoxybenzanthrone (MBA) and 8-anilino-1-naphthalene sulfonic acid (ANS) as acceptors has been examined to obtain information on the structure of peptide-lipid systems consisting of 18A or Ac-18A-NH 2 peptides and large unilamellar phosphatidylcholine vesicles. The lower and upper...
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