| Summary: | Gramicidin A' (GA') has been added to three lipid systems of varying hydrophobic thicknesses: dimyristoyllecithin (DML), dipalmitoyllecithin (DPL), and distearoyllecithin (DSL). The similarity in length between the hydrophobic portion of GA' and the hydrocarbon chains of the lipid bilayers has been studied by using ^(31)P and ^2H NMR. Hydrophobic mismatch has been found to be most severe in the DML bilayer system and minimal in the case of DSL. In addition, the effects of hydrophobic mismatch on the cooperative properties of the bilayer have been obtained from ^2H NMR relaxation measurements. The results indicate that incorporation of the peptide into the bilayer disrupts the cooperative director fluctuations characteristic of pure multilamellar lipid dispersions. Finally, the GA'llecithin ratio at which the well-known transformation from bilayer to reverse hexagonal (H_(II)) phase occurs (Van Echteld et al., 1982; Chupin et al., 1987) is shown to depend on the acyl chain length of the phospholipid. A rationale is proposed for this chain length dependence. © 1990 American Chemical Society. Published in print 3 July 1990. Contribution No. 8343 of the Division of Chemistry and Chemical Engineering, California Institute of Technology. This work was supported by Grants GM-22432 (S.I.C.), GM-36132 (P.D.), and RR-08101 (P.D.) from the National Institutes of General Medical Sciences, US. Public Health Service, and by the donors of the Petroleum Research Fund, administered by the American Chemical Society. P.I.W. was a recipient of a National Research Service Award (T32 GM07616) from the National Institutes of General Medical Sciences. Access to the Southern California Regional NMR Facility at Caltech, supported by National Science Foundation Grant CHE84-40137, for the NMR experiments is gratefully acknowledged. We thank Drs. T. Handel, A. Nayeem, H. Eckert, and J. Yesinowski for helpful discussions and assistance.
|
|---|