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Direct Determination of a Membrane-Peptide Interface Using the Nuclear Magnetic Resonance Cross-Saturation Method

Takefumi Nakamura ^*, Hideo Takahashi , Koh Takeuchi , Toshiyuki Kohno , Kaori Wakamatsu ^¶ and Ichio Shimada  

^* Japan Biological Information Research Center, Japan Biological Informatics Consortium, Tokyo 135-0064, Japan; Biological Information Research Center, National Institute of Advanced Industrial Science and Technology, Tokyo 135-0064, Japan; Graduate School of Pharmaceutical Sciences, University of Tokyo, Tokyo 113-0033, Japan; Mitsubishi Kagaku Institute of Life Sciences, Tokyo 194-8511, Japan; and ^¶ Department of Biochemical and Chemical Engineering, Gunma University, Gunma 376-8515, Japan

Correspondence: Address reprint requests to Dr. Hideo Takahashi, Tel.: 81-3-3599-8112; Fax: 81-3-3599-8099; E-mail: hid{at}jbirc.aist.go.jp; or to Prof. Ichio Shimada, Tel.: 81-3-5841-4810; Fax: 81-3-3815-6540; E-mail: shimada{at}iw-nmr.f.u-tokyo.ac.jp.

Membrane-peptide interactions are involved in many crucial biological and pharmacological activities. To clarify the interaction mode of membrane-peptide complexes, it is important to analyze both the dynamic properties and the contact residues of the membrane-bound peptide. In this study, we investigated the dynamic properties of a peptide bound to a lipid bilayer, using relaxation and amide-water exchange analyses, and directly determined the membrane-peptide interface, using the cross-saturation method. For the models of a lipid bilayer and a peptide, isotropic bicelles and mastoparan were used, respectively. The results indicate that mastoparan had a heterogeneous distribution of motion over various timescales and interacted with the lipid bilayer by using its hydrophobic side; the molecule was located within the lipid bilayer rather than on the surface, as thought previously. This study shows that the cross-saturation method is useful for determining the interface of not only protein-protein but also membrane-peptide complexes.

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