Solvent polarity-dependent structural refolding: a CD and NMR study of a 15 residue peptide

Proteins
A Graf von StoschJ Reed

Abstract

A close association between the HIV surface protein gp120 and the CD4 T cell receptor initiates the viral multiplication cycle. A 15 amino acid peptide (LAV) within the CD4 binding domain of gp 120 has been shown to retain receptor binding ability. The structural behavior of the LAV peptide has been studied by CD and NMR methods in aqueous solution and upon addition of trifluoroethanol (TFE) to emulate the relatively apolar conditions at the membrane bound receptor. Previous work has shown that the LAV peptide folds into a beta-pleated structure in more polar buffer/TFE mixtures, while a concerted structural change can be observed at a concentration of 60% TFE (v/v). This abrupt, cooperative refolding from a regular beta-sheet to a helical secondary structure is known as "switch" behavior. Former CD experiments with LAV sequence variants have supported the assumption that four amino acids at the N-terminus (LPCR) are indispensable for the "switch." The tetrad has a strong beta-turn forming potential. The suggestion has been formulated that the tetrad can act as a nucleation site governing the refolding. The present NMR study of the LAV peptide in TFE gives evidence for a 3(10)-helix suggesting that the tetrad adopts a type III ...Continue Reading

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Citations

Feb 1, 1997·Journal of Biomolecular Structure & Dynamics·Y van BoulangerG Sauvé
Jul 29, 2008·Biophysical Journal·Nasrollah Rezaei-GhalehMohsen Nemat-Gorgani
Feb 27, 2007·Analytical Biochemistry·Bernhard C PoschnerMathias W Hofmann
Dec 19, 2012·International Journal of Biological Macromolecules·Ganesh ShanmugamBalaraman Madhan
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