2019 年 59 巻 6 号 p. 310-313
Biophysical characterizations of membrane properties are performed for a series of novel partially fluorinated dimyristoylphosphatidylcholines with different perfluoroalkyl (Rf, CnF2n+1) chain lengths (Fn-DMPC) developed as possible materials for incorporating membrane proteins. The Fn-DMPC membranes exhibit thermal chain-melting transition in a significant Rf-chain length-dependent manner. It is of note that F8-DMPC, whose perfluorooctyl groups are likely to aggregate into the hexagonal structure, shows the notably high transition temperature of 64.4°C compared to 24.1°C for DMPC. Reconstituted bacteriorhodopsin molecules in F4-DMPC membrane adopt native-like higher-order structure and photocycle both in the gel and the fluid phases.