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Biophys. J. BioFAST: First Published December 9, 2005. doi:10.1529/biophysj.105.073858
© 2005 by the Biophysical Society.

A more recent version of this article appeared on March 1, 2006.
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MEMBRANES

Solid-state NMR analysis of the PGLa peptide orientation in DMPC bilayers: structural fidelity of 2H-labels versus high sensitivity of 19F-NMR

Erik Strandberg 1, Pierre Tremouilhac 1, Parvesh Wadhwani 1, Ulrich H. N. Dürr 2 and Anne S. Ulrich 2*

1 Forschungszentrum Karlsruhe
2 University of Karlsruhe

* To whom correspondence should be addressed. E-mail: anne.ulrich{at}ibg.fzk.de.

Submitted on September 7, 2005
Revised on September 29, 2005
Accepted on 17 November 2005


  Abstract
The structure and alignment of the amphipathic {alpha}-helical antimicrobial peptide PGLa in a lipid membrane is determined with high accuracy by solid-state 2H-NMR. Orientational constraints are derived from a series of eight Ala-d3 labeled peptides, in which either a native alanine is non-perturbingly labeled (4x), or a glycine (2x) or isoleucine (2x) is selectively replaced. The concentration dependent re-alignment of the {alpha}-helix from the surface-bound "S-state" to a tilted "T-state" by 30° is precisely calculated using the quadrupole splittings of the four non-perturbing labels as constraints. The remaining, potentially perturbing Ala-d3 labels show only minor deviations from the unperturbed peptide structure and help to single out the unique solution. Comparison with previous 19F-NMR constraints from 4-CF3-phenylglycine labels shows that the structure and orientation of the PGLa peptide is not much disturbed even by these bulky non-natural side chains, which contains CF3 groups that offer a 20-fold better NMR sensitivity than CD3 groups.

Key Words: DMPC model membranes, antimicrobial peptide PGLa, deuterium quadrupole splittings, helix alignment, homonuclear fluorine dipolar couplings, solid-state deuterium NMR




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Copyright © 2005 by the Biophysical Society.