[12p-PA6-1~15] 12.6 Nanobiotechnology

[12p-PA6-9] Elucidation of the contribution of hydrophobic matching in partitioning membrane proteins into lipid bilayer domains

Kazuha Shimizu¹, Hiroka Hatano², Hitoshi Asakawa², 〇Toshinori Motegi¹ (1.Gunma Univ., 2.Kanazawa Univ.)

Keywords:lipid bilayer membrane, atomic force microscopy, membrane protein

Membrane proteins in biological membranes are involved in physiological phenomena such as intracellular and extracellular substance transport and immune functions. For the expression of membrane protein function, a domain in which specific lipids and membrane proteins are assembled is essential. Previous our studies have directly shown that in the partitioning of membrane proteins into domains, the hydrophobic matching effect and the charge between lipids and membrane proteins are important factors. On the other hand, the difference in the hydrophobic matching effect between the case where the lipid hydrophobic part is short and the case where the lipid hydrophobic part is long compared to the hydrophobic part of the membrane protein has not been studied much. In this study, by the investigation of the structure and localization of a model membrane protein, bacteriorhodopsin (bR), in a substrate-supported artificial lipid bilayer (SLB) composed of lipids of different hydrophobic lengths, we aimed to elucidate the contribution of domains to membrane protein localization.