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Chem Phys Lipids. 1998 Jul;94(1):81-96.

Interaction of a basic amphipathic peptide from the carboxyterminal part of the HIV envelope protein gp41 with negatively charged lipid surfaces.

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Institute of Biochemistry, Westfälische Wilhelms-Universität Münster, Germany.


The interaction of the positively charged synthetic amphipathic peptide fragment gp41(828) corresponding to a segment from the carboxyterminal region of the HIV envelope glycoprotein gp41 with lipid monolayers spread at the air-water interface has been studied by film balance measurements. The peptide itself does not form a stable monolayer but interacts with phospholipids spread together on the aqueous surface. Upon compression of a mixed phosphatidylcholine-peptide monolayer the peptide is irreversibly squeezed out of the lipid-peptide monolayer. In contrast, with negatively charged phosphatidylglycerol stable lipid-peptide monolayers are formed even in the presence of up to 30 mol% peptide. The monolayer may be expanded and compressed repeatedly without significant loss of substance. After addition of calcium ions to the subphase of a phosphatidylglycerol-peptide monolayer the peptide is to some extent excluded from the monolayer. In contrast to phosphatidylcholine monolayers this process is partly reversible and the excluded material is reincorporated into the film during subsequent expansion. We conclude that attached to the headgroups of the lipid monolayer a peptide-layer stabilized at the surface by electrostatic interactions is formed. The surface action may lead to rigidified lipid-peptide domains causing an increased membrane permeability which might correspond to a cytopathologic function of the protein fragment.

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