Interaction of short modified peptides deriving from glycoprotein gp36 of feline immunodeficiency virus with phospholipid membranes |
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Authors: | Gerardino D’Errico Giuseppe Vitiello Anna Maria D’Ursi Derek Marsh |
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Institution: | 1.Dipartimento di Chimica “Paolo Corradini”,Università di Napoli “Federico II”,Naples,Italy;2.Dipartimento di Scienze Farmaceutiche,Università di Salerno,Fisciano,Italy;3.Abt Spektroskopie,Max-Planck-Institut für biophysikalische Chemie,G?ttingen,Germany |
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Abstract: | A tryptophan-rich octapeptide, C8 (Ac-Trp-Glu-Asp-Trp-Val-Gly-Trp-Ile-NH2), modelled on the membrane-proximal external region of the feline immunodeficiency virus (FIV) gp36 glycoprotein ectodomain,
exhibits potent antiviral activity against FIV. A mechanism has been proposed by which the peptide, being positioned on the
surface of the cell membrane, inhibits its fusion with the virus. In the present work, peptide–lipid interactions of C8 with
dimyristoyl phosphatidylcholine liposomes are investigated using electron spin resonance spectroscopy of spin-labelled lipids.
Three other peptides, obtained from modifications of C8, have also been investigated, in an attempt to clarify the essential
molecular features of the interactions involving the tryptophan residues. The results show that C8 adsorbs strongly on the
bilayer surface. Membrane binding requires not only the presence of the Trp residues in the sequence, but also their common
orientation on one side of the peptide that is engendered by the WX2 WX2 W motif. Membrane interaction correlates closely with peptide antiviral activity, indicating that the membrane is essential
in stabilizing the peptide conformation that will be able to inhibit viral infection. |
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Keywords: | Feline immunodeficiency virus Membrane Electron spin resonance Spin-label |
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