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J. Biol. Chem., Vol. 281, Issue 12, 7708-7716, March 24, 2006

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Interactions Involved in the Realignment of Membrane-associated Helices

AN INVESTIGATION USING ORIENTED SOLID-STATE NMR AND ATTENUATED TOTAL REFLECTION FOURIER TRANSFORM INFRARED SPECTROSCOPIES^*

Christopher Aisenbrey¹, Rudolf Kinder¹, Erik Goormaghtigh^¶, Jean-Marie Ruysschaert^¶, and Burkhard Bechinger²

From the Institut/Faculté de Chimie, Université Louis Pasteur/CNRS LC3-UMR7177, 4 Rue Blaise Pascal, Strasbourg 67070, France, Max-Planck-Institut für Biochemie, Am Klopferspitz 18A, 82152 Martinsried, Germany, and ^¶Laboratory for the Structure and Function of Biological Membranes, Center for Structural Biology and Bioinformatics, Université Libre Bruxelles, Campus Plaine CP206/2, Brussels 1050, Belgium

A series of histidine-containing peptides (LAH₄X₆) was designed to investigate the membrane interactions of selected side chains. To this purpose, their pH-dependent transitions from in-plane to transmembrane orientations were investigated by attenuated total reflection Fourier transform infrared and oriented solid-state NMR spectroscopies. Peptides of the same family have previously been shown to exhibit antibiotic and DNA transfection activities. Solution NMR spectroscopy indicates that these peptides form amphipathic helical structures in membrane environments, and the technique was also used to characterize the pK values of all histidines in the presence of detergent micelles. Whereas one face of the amphipathic helix is clearly hydrophobic, the opposite side is flanked by four histidines surrounding six leucine, alanine, glycine, tryptophan, or tyrosine residues, respectively. This diversity in peptide composition causes pronounced shifts in the midpoint pH of the in-plane to transmembrane helical transition, which is completely abolished for the peptides carrying the most hydrophilic amino acid residues. These properties open up a conceptually new approach to study in a quantitative manner the hydrophobic as well as specific interactions of amino acids in membranes. Notably, the resulting scale for whole residue transitions from the bilayer interface to the hydrophobic membrane interior is obtained from extended helical sequences in lipid bilayers.

Received for publication, December 9, 2005 , and in revised form, January 3, 2006.

^* This work was supported by the Agence Nationale pour la Recherche contre le SIDA, Vaincre la Mucoviscidose, Deutsche Forschungsgemeinschaft Grant SFB 266, CNRS, the Université Louis Pasteur, and the French Ministry of Research. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. 7–9 and Equations 5–8.

¹ These authors contributed equally to this work.

² To whom correspondence should be addressed. Tel.: 33-3-90-24-51-50; Fax: 33-3-90-24-51-51; E-mail: bechinger{at}chimie.u-strasbg.fr.

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