Membrane properties of ether-type phosphatidylcholine bearing partially fluorinated C 18 -monoacetylenic chains and their applicability to membrane protein reconstitution matrices

• Published in: Colloids and surfaces, B, Biointerfaces B, Biointerfaces, 2021-02, Vol.198, p.111459
• Main Authors: Baba, Teruhiko, Takagi, Toshiyuki, Sumaru, Kimio, Kanamori, Toshiyuki, Dewa, Takehisa, Nango, Mamoru
• Format: Article
• Language: English
• ISSN: 1873-4367
• DOI: 10.1016/j.colsurfb.2020.111459

To examine the applicability of fluorinated membrane-forming phospholipids to reconstitution matrices for functional membrane proteins, the membrane properties of a synthetic ether-type phosphatidylcholine (PC) bearing partially fluorinated C -monoacetylenic (9-octadecynyl) chains, DF CCH PC, were compared with those of its non-fluorinated counterpart, DH CCH PC. Light-harvesting complex 2 (LH2) and the light-harvesting 1‒reaction center core complex (LH1-RC) isolated from purple photosynthetic bacteria were employed as probe membrane proteins to evaluate the extent to which their reconstitution into DF CCH PC membranes could proceed. DF CCH PC formed more expanded and more stable fluid monolayers than DH CCH PC at the air-water interface at 25 °C; the former PC molecule occupied an area of ca. 0.70 nm at a collapse pressure, π , of 52 mN/m, while the latter occupied an area of ca. 0.55 nm at a π of 45 mN/m. In contrast, the molecular motion detected using fluorescent probes was much more restricted in DF CCH PC bilayers than in DH CCH PC ones. Although the reconstitution efficiencies of both LH2 and LH1-RC into DF CCH PC bilayers were lower than those into DH CCH PC bilayers, the membrane proteins incorporated into DF CCH PC bilayers showed increased thermostability. The increased thermostability of these proteins in fluorinated PC membranes might be due to the restricted molecular motion in the hydrophobic chains. The results of this study suggest that partially fluorinated PCs can be useful materials for the construction of lipid‒functional membrane protein assemblies including large membrane protein complexes, such as LH1-RC, for biotechnological applications.