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The influence of cholesterol on the interaction of HIV gp41 membrane proximal region‐derived peptides with lipid bilayers
Author(s) -
Veiga Ana S.,
Castanho Miguel A. R. B.
Publication year - 2007
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2007.06029.x
Subject(s) - ectodomain , peptide , membrane , peptide sequence , chemistry , biophysics , biology , biochemistry , receptor , gene
A small amino acid sequence (LWYIK) inside the HIV‐1 gp41 ectodomain membrane proximal region (MPR) is commonly referred to as a cholesterol‐binding domain. To further study this unique and peculiar property we have used fluorescence spectroscopy techniques to unravel the membrane interaction properties of three MPR‐derived synthetic peptides: the membrane proximal region peptide‐complete (MPRP‐C) which corresponds to the complete MPR; the membrane proximal region peptide‐short (MPRP‐S), which corresponds to the last five MPR amino acid residues (the putative cholesterol‐binding domain) and the membrane proximal region peptide‐intermediate (MPRP‐I), which corresponds to the MPRP‐C peptide without the MPRP‐S sequence. MPRP‐C and MPRP‐I membrane interaction is largely independent of the membrane phase. Membrane interaction of MPRP‐S occurs for fluid phase membranes but not in gel phase membranes or cholesterol‐containing bilayers. The gp41 ectodomain MPR may have a very specific function in viral fusion through the concerted and combined action of cholesterol‐binding and non‐cholesterol‐binding domains (i.e. domains corresponding to MPRP‐S and MPRP‐I, respectively).