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Hydrophobic mismatch in gramicidin A prime /lecithin systems

Journal Article · · Biochemistry; (USA)
DOI:https://doi.org/10.1021/bi00478a015· OSTI ID:6229739
;  [1];  [2]
  1. California Institute of Technology, Pasadena (USA)
  2. California State Univ., Los Angeles (USA)
Gramicidin A{prime} (GA{prime}) has been added to three lipid systems of varying hydrophobic thickness: dimyristoyllecithin (DML), dipalmitoyllecithin (DPL), and distearoyllecithin (DSL). The similarity in length between the hydrophobic portion of GA{prime} and the hydrocarbon chains of the lipid bilayers has been studied by using {sup 31}P and {sup 2}H 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 {sup 2}H 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{prime}/lecithin ratio at which the well-known transformation from bilayer to reverse hexagonal (H{sub II}) phase occurs is shown to depend on the acyl chain length of the phospholipid. A rationale is proposed for this chain length dependence.
OSTI ID:
6229739
Journal Information:
Biochemistry; (USA), Journal Name: Biochemistry; (USA) Vol. 29:26; ISSN 0006-2960; ISSN BICHA
Country of Publication:
United States
Language:
English