Direct determination of a membrane-peptide interface using the nuclear magnetic resonance cross-saturation method.
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.
Nakamura
Takefumi
T
Japan Biological Information Research Center, Japan Biological Informatics Consortium, Tokyo 135-0064, Japan.
Takahashi
Hideo
H
Takeuchi
Koh
K
Kohno
Toshiyuki
T
Wakamatsu
Kaori
K
Shimada
Ichio
I
D000465:Algorithms; D036341:Intercellular Signaling Peptides and Proteins; D008051:Lipid Bilayers / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008565:Membrane Proteins / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D011485:Protein Binding; D013499:Surface Properties; D014862:Wasp Venoms / Q000737:chemistry*; D014867:Water / Q000737:chemistry*
D036341:Intercellular Signaling Peptides and Proteins; D008051:Lipid Bilayers; D008565:Membrane Proteins; D010455:Peptides; D014862:Wasp Venoms; D014867:Water; C037500:mastoparan