title: Dynamic properties of gramicidin A in phospholipid membranes.
abstract: The flexibility of the tryptophan side chains of gramicidin A and the rotational diffusion of the peptide in methanolic solution and in three membrane systems were studied with deuterium nuclear magnetic resonance (NMR). Gramicidin A was selectively deuterated at the aromatic ring systems of its four tryptophan side chains. In methanolic solution, the tryptophan residues remained immobile and served as a probe for the overall rotation of the peptide. The experimentally determined rotational correlation time of tau c = 0.6 X 10(-9) s was consistent with the formation of gramicidin A dimers. For gramicidin A incorporated into bilayer membranes, quite different results were obtained depending on the chemical and physical nature of the lipids employed. When mixed with 1-palmitoyl-sn-glycero-3-phosphocholine (LPPC) at a stoichiometric lipid:peptide ratio of 4:1, gramicidin A induced the formation of stable bilayer membranes in which the lipids were highly fluid. In contrast, the gramicidin A molecules of this membrane remained completely static over a large temperature interval, suggesting strong protein-protein interactions. The peptide molecules appeared to form a rigid two-dimensional lattice in which the interstitial spaces were filled with fluidlike lipids. When gramicidin A was incorporated into bilayers of 1,2-dioleoyl-sn-glycero-3-phosphocholine or 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) above the lipid phase transition, the deuterium NMR spectra were motionally narrowed, indicating large-amplitude rotational fluctuations. From the measurement of the quadrupole echo relaxation time, a rotational correlation time of 2 X 10(-7) s was estimated, leading to a membrane viscosity of 1-2 P if the rotational unit was assumed to be a gramicidin A dimer. (ABSTRACT TRUNCATED AT 250 WORDS)
authors: Department of Biophysical Chemistry, Biocenter of the University of Basel, Switzerland.
authors: P M
authors: PM
authors: Macdonald
authors: J
authors: J
authors: Seelig
mesh_terms: D004134:Dimyristoylphosphatidylcholine; D006096:Gramicidin; D008081:Liposomes; D008244:Lysophosphatidylcholines; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008954:Models, Biological; D008968:Molecular Conformation; D013816:Thermodynamics
chemical_list: D008081:Liposomes; D008244:Lysophosphatidylcholines; D006096:Gramicidin; C006065:We 201; D004134:Dimyristoylphosphatidylcholine