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Lipid Bilayer Perturbations Induced by Simple Hydrophobic Peptides

Jacobs, Russell E. and White, Stephen H. (1987) Lipid Bilayer Perturbations Induced by Simple Hydrophobic Peptides. Biochemistry, 26 (19). pp. 6127-6134. ISSN 0006-2960. https://resolver.caltech.edu/CaltechAUTHORS:20160516-112833897

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Abstract

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 ([^2H_(54))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/T_1(i), exhibit a square-law functional dependence on S_(CD)(i) both with and without the addition of peptide. The addition of peptide causes an increase in the slope of plots of 1/T_1(i)vs. │S_(CD)(i)│_2 with little change in the 1/T_1(i) intercept, indicating a complex modulation of the acyl chain motions. ^2H NMR spectra of Ala-[^2H_4]Ala-Ala-O-tert-butyl in DMPC bilayers have both isotropic and powder pattern components that vary as a function of temperature. At 30 °C the ^2H spin-lattice relaxation times for the labeled Ala residue increase in going from bilayerincorporated peptide to polycrystalline peptide to polycrystalline Ala·HCI. These experiments provide no information on the location of these peptides in the bilayer. If they protrude into the hydrocarbon core, their disordering influence can be attributed to a direct disruption of acyl chain packing. If they are adsorbed to the bilayer surface, their influence on the bilayer interior must be an indirect disruption propagated via the head group region.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1021/bi00393a027DOIArticle
http://pubs.acs.org/doi/abs/10.1021/bi00393a027PublisherArticle
ORCID:
AuthorORCID
Jacobs, Russell E.0000-0002-1382-8486
Additional Information:© 1987 American Chemical Society. Received December 10, 1986; Revised Manuscript Received May 18, 1987. This work was supported by grants from the National Institutes of Health (RR 01993) and the National Science Foundation (DMB-8412754). We thank April Diaz for synthesis of the peptides. We are especially grateful to Drs. Edward Sternin and Myer Bloom for a listing of their de-Paking routine and to Dr. Jay Edleman for assistance in implementing it on our computer system.
Funders:
Funding AgencyGrant Number
NIHRR 01993
NSFDMB-8412754
Issue or Number:19
Record Number:CaltechAUTHORS:20160516-112833897
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20160516-112833897
Official Citation:Lipid bilayer perturbations induced by simple hydrophobic peptides Russell E. Jacobs and Stephen H. White Biochemistry 1987 26 (19), 6127-6134 DOI: 10.1021/bi00393a027
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:67130
Collection:CaltechAUTHORS
Deposited By: Ruth Sustaita
Deposited On:16 May 2016 21:50
Last Modified:03 Oct 2019 10:03

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