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. 2004 Apr 28;126(16):5078-9.
doi: 10.1021/ja032015d.

A new method for determining the local environment and orientation of individual side chains of membrane-binding peptides

Matthew J Tucker  1 , Zelleka Getahun, Vikas Nanda, William F DeGrado, Feng Gai
Affiliations

A new method for determining the local environment and orientation of individual side chains of membrane-binding peptides

Matthew J Tucker et al. J Am Chem Soc. .

Abstract

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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