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Lipid-Gramicidin Interactions: Dynamic Structure of the Boundary Lipid by 2D-ELDOR

Department of Chemistry and Chemical Biology and National Biomedical Center for Advanced ESR Technology, Cornell University, Ithaca, New York 14853-1301 USA

Correspondence: Address reprint requests to Prof. Jack H. Freed, Dept. of Chemistry and Chemical Biology, B52 Baker Laboratory, Cornell University, Ithaca, NY 14853. Tel.: 607-255-3647; Fax: 607-255-0595; E-mail: jhf{at}ccmr.cornell.edu.

The use of 2D-electron-electron double resonance (2D-ELDOR) for the characterization of the boundary lipid in membrane vesicles of DPPC and gramicidin A' (GA) is reported. We show that 2D-ELDOR, with its enhanced spectral resolution to dynamic structure as compared with continuous-wave electron spin resonance, provides a reliable and useful way of studying lipid-protein interactions. The 2D-ELDOR spectra of the end-chain spin label 16-PC in DPPC/GA vesicles is composed of two components, which are assigned to the bulk lipids (with sharp auto peaks and crosspeaks) and to the boundary lipids (with broad auto peaks). Their distinction is clearest for higher temperatures and higher GA concentrations. The quantitative analysis of these spectra shows relatively faster motions and very low ordering for the end chain of the bulk lipids, whereas the boundary lipids show very high "y-ordering" and slower motions. The y-ordering represents a dynamic bending at the end of the boundary lipid acyl chain, which can then coat the GA molecules. These results are consistent with the previous studies by Ge and Freed (1999) using continuous-wave electron spin resonance, thereby supporting their model for GA aggregation and H_II phase formation for high GA concentrations. Improved instrumental and simulation methods have been employed.

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