Membrane destabilization induced by the human immunodeficiency virus type-1 fusion peptide |
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Authors: | José L. Nieva Félix M. Goñi Arturo Muga Shlomo Nir Francisca Pereira |
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Affiliation: | (1) Department of Biochemistry (Grupo de Biomembranas, Unidad Asociada al CSIC), University of the Basque Country, P.O. Box 644, E-48080 Bilbao, Spain;(2) Seagram Center for Soil and Water Sciences, Faculty of Agriculture, The Hebrew University of Jerusalem, 76100 Rehovot, Israel |
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Abstract: | Summary The human immunodeficiency virus type-1 (HIV-1) fusion peptide, corresponding to a sequence of 23 amino acid residues at the N-terminus of the spike transmembrane subunit gp41, has the capacity to destabilize negatively charged and neutral large unilamellar vesicles, representing, respectively, the acidic and the neutral fraction of the plasma membrane lipids of viral target cells. As revealed by infrared spectroscopy, the peptide associated with the vesicles may exist in different conformations. In negatively charged membranes the structure is mainly an α-helix, while in Ca2+-neutralized negatively charged membranes the conformation switches to a predominantly extended conformation. In membranes composed of zwitterionic phospholipids and cholesterol, the peptide also adopts a predominant extended structure. The α-helical structure permeabilizes negatively charged vesicles but does not induce membrane fusion. The peptide in β-type conformation, on the other hand, permeabilizes neutral membranes and triggers fusion. As seen by31P NMR, the latter structure also exhibits the capacity to alter the lamellar organization of the membrane. |
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Keywords: | Conformational switching Membrane fusion Peptide conformation Peptide-lipid interaction |
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