The interaction of helical polypeptides with biological model membranes

ISSN： 1066-5285

Source： Russian Chemical Bulletin, Vol.53, Iss.7, 2004-07, pp. : 1428-1433

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Abstract

Proton-decoupled solid-state ¹⁵N NMR spectroscopy was used to investigate helical peptides reconstituted into oriented phospholipid bilayers. Hydrophobic channel peptides such as the N-terminal region of Vpu of human immunodeficiency virus (HIV-1) adopt transmembrane orientations, whereas amphipathic peptide antibiotics are oriented parallel to the bilayer surface. The alignment of helical peptides in lipid membranes was analysed in some detail using model peptides. In particular, peptides with pH-dependent topology and a series of peptides that allow one to study the contributions of specific interactions were designed. The energies of transfer of several amino acids from the in-plane to transmembrane localisation were determined. In addition, the alignment of peptides and phospholipids under conditions of hydrophobic mismatch have been investigated in considerable detail.