Lipid−Protein Nanoscale Bilayers:  A Versatile Medium for NMR Investigations of Membrane Proteins and Membrane-Active Peptides

• Published in: Journal of the American Chemical Society 2008-02, Vol.130 (7), p.2140-2141
• Main Authors: Lyukmanova, Ekaterina N, Shenkarev, Zakhar O, Paramonov, Alexander S, Sobol, Alexander G, Ovchinnikova, Tatiana V, Chupin, Vladimir V, Kirpichnikov, Mikhail P, Blommers, Marcel J. J, Arseniev, Alexander S
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Apolipoprotein A-I - chemistry; Lipid Bilayers - chemistry; Membrane Proteins - chemistry; Molecular Sequence Data; Nanostructures - chemistry; Nuclear Magnetic Resonance, Biomolecular - methods; Peptides - chemistry; Phosphatidylcholines - chemistry; Phosphatidylglycerols - chemistry; Phospholipids - chemistry
• ISSN: 0002-7863; 1520-5126
• DOI: 10.1021/ja0777988

In the present Communication we demonstrate the possibility to use high-resolution NMR for the investigation of membrane proteins in reconstituted high-density lipoprotein (rHDL) particles. The rHDL particles are nanoscale phospholipid bilayers wrapped around by a dimer of apolipoprotein A-1 (Bayburt, T. H.; Grinkova, Y. V.; Sligar, S. G. Nano Lett. 2002, 2, 853−856). In contrast to the commonly used spherical micelles, the rHDL particles incorporate a lipid bilayer like in biological membranes. These particles still undergo isotropic motion on the NMR time scale, providing the application of high-resolution NMR spectroscopy of the peptides and proteins embedded into their bilayer. As an example, the topology of the membrane-active peptide Antiamoebin-I in the bilayer of the rHDL particles was determined by using the lipid-soluble relaxation probe technique.