A New Method for Determining the Local Environment and Orientation of Individual Side Chains of Membrane-Binding Peptides

Matthew J. Tucker, Zelleka Getahun, Vikas Nanda, William F. DeGrado,* and Feng Gai*;
Department of Chemistry and Department of Biochemistry & Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19104
J. Am. Chem. Soc., 2004, 126 (16), pp 5078–5079
DOI: 10.1021/ja032015d
Publication Date (Web): April 2, 2004
Copyright © 2004 American Chemical Society

Abstract

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We studied here the binding of the mastoparan X peptide to a zwitterionic lipid bilayer (POPC) and demonstrated that nitrile-derivatized amino acids can be used to determine the hydration state (or change in hydration state) of specific sites of membrane-interactive peptides (upon binding). We have also shown that polarized ATR-FTIR measurements can further be used to uncover information regarding the spatial orientation of individual side chains as well as their conformational preference within the lipid bilayer.

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History

  • Published In Issue April 28, 2004
  • Received December 31, 2003

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