Jacobs R E, White S H
Department of Physiology & Biophysics, University of California, Irvine 92717.
Biochemistry. 1987 Sep 22;26(19):6127-34. doi: 10.1021/bi00393a027.
Mixtures of tripeptides of the form Ala-X-Ala-O-tert-butyl with 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) bilayers have been used as a model system for studying the influence of hydrophobic peptides on membrane order and dynamic properties by means of deuterium NMR spectroscopy. Tripeptides with X = Ala, Leu, Phe, and Trp have been examined. Lipid 2H NMR spectra of acyl chain perdeuteriated DMPC ([2H54]DMPC) show that the addition of peptide disorders the bilayer lipid acyl chains and that the extent of the perturbation increases as the size of the central residue increases. Moment analyses of the spectra indicate that, while the average acyl chain order parameter decreases with increasing central residue size, the order parameter spread across the bilayer (the mean-squared width of the distribution) increases. Lipid segmental 2H longitudinal relaxation rates, 1/T1(i), exhibit a square-law functional dependence on SCD(i) both with and without the addition of peptide. The addition of peptide causes an increase in the slope of plots of 1/T1(i) vs. (SCD(i))2 with little change in the 1/T1(i) intercept, indicating a complex modulation of the acyl chain motions. 2H NMR spectra of Ala-[2H4]Ala-Ala-O-tert-butyl in DMPC bilayers have both isotropic and powder pattern components that vary as a function of temperature. At 30 degrees C the 2H spin-lattice relaxation times for the labeled Ala residue increase in going from bilayer-incorporated peptide to polycrystalline peptide to polycrystalline Ala.HCl. These experiments provide no information on the location of these peptides in the bilayer.(ABSTRACT TRUNCATED AT 250 WORDS)
