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Originally published as Biophys J. BioFAST on December 9, 2005.
doi:10.1529/biophysj.105.073858
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Biophysical Journal 90:1676-1686 (2006)
© 2006 The Biophysical Society

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 *, Parvesh Wadhwani *, Pierre Tremouilhac *, Ulrich H. N. Dürr {dagger} and Anne S. Ulrich * {dagger}

* Institute for Biological Interfaces, Forschungszentrum Karlsruhe, 76344 Eggenstein-Leopoldshafen, Germany; and {dagger} Institute of Organic Chemistry, University of Karlsruhe, 76131 Karlsruhe, Germany

Correspondence: Address reprint requests to Anne S. Ulrich, E-mail: anne.ulrich{at}ibg.fzk.de.

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 alanine-3,3,3-d3-labeled peptides, in which either a native alanine is nonperturbingly labeled (4x), or a glycine (2x) or isoleucine (2x) is selectively replaced. The concentration dependent realignment 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 nonperturbing labels as constraints. The remaining, potentially perturbing alanine-3,3,3-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 nonnatural side chains, which contain CF3 groups that offer a 20-fold better NMR sensitivity than CD3 groups.




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