2017 年 42 巻 5 号 p. 202-206
Lipid nanodiscs are discoidal particles with a planar phospholipid bilayer enwrapped by polypeptide chains such as apolipoprotein A–I, membrane scaffold protein (MSP), and amphiphilic class A α– helical peptides. Nanodiscs have been widely used for analyzing structures and functions of membrane proteins by dispersing them in solution. They are expected to be used as drug carriers and therapeutic agents. This review focuses on the nanodisc-forming amphiphilic peptides. An amphiphilic self–polymerizing peptide termed ASPP1, which polymerizes by intermolecular native chemical ligation, was synthesized. ASPP1 spontaneously formed nanodiscs when added to phospholipid vesicles without using detergents. The diameter of the planar lipid bilayer in the nanodiscs was controlled within a range of 15 to 30 nm by the lipid : peptide molar ratio. ASPP1–nanodiscs exhibited greater stability at high temperatures or in the presence of urea than nanodiscs formed by the non–polymerizing amphiphilic peptide or apolipoprotein A–I. These results show that the lipid–peptide nanodiscs provide promise for future applications.