CaltechAUTHORS
  A Caltech Library Service

Mixtures of a Series of Homologous Hydrophobic Peptides with Lipid Bilayers: A Simple Model System for Examining the Protein-Lipid Interface

Jacobs, Russell E. and White, Stephen H. (1986) Mixtures of a Series of Homologous Hydrophobic Peptides with Lipid Bilayers: A Simple Model System for Examining the Protein-Lipid Interface. Biochemistry, 25 (9). pp. 2605-2612. ISSN 0006-2960. https://resolver.caltech.edu/CaltechAUTHORS:20160516-132218945

Full text is not posted in this repository. Consult Related URLs below.

Use this Persistent URL to link to this item: https://resolver.caltech.edu/CaltechAUTHORS:20160516-132218945

Abstract

The interactions of several members of a homologous series of peptides with the phospholipid bilayer have been examined by using fluorescence and deuterium NMR spectroscopy, differential scanning calorimetry, and measurements of water-to-bilayer partition coefficients. 1,2-Dimyristoyl-sn-glycero-3- phosphocholine (DMPC) bilayers and tripeptides of the form Ala-X-Ala-O-tert-butyl are used as a model system to probe the influence of amino acid side-chain substitution on the insertion of peptides into membranes and the behavior of peptide/bilayer mixtures. Tripeptides with X = Gly, Ala, Phe, and Trp have been examined. All of the tripeptides are water soluble, and all partition into DMPC bilayer vesicles to some extent. The Gly-containing peptide is the least soluble and the Trp-containing peptide the most soluble in the bilayer. The extent of perturbation of the bilayer structure induced by the peptides parallels their bilayer solubility: the Gly and Ala peptides act as simple impurities while peptides containing bulky aromatic rings cause a phase separation. Changes in the fluorescence properties of the Trp analogue upon incorporation into the bilayer indicate that the Trp side chain is probably immersed in the hydrocarbon region of the bilayer. Peptides of this form should serve as easily modifiable model systems with which to examine details of how the bilayer environment affects peptide conformation, as well as how hydrophobic peptides affect the bilayer structure.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1021/bi00357a049DOIArticle
http://pubs.acs.org/doi/abs/10.1021/bi00357a049PublisherArticle
ORCID:
AuthorORCID
Jacobs, Russell E.0000-0002-1382-8486
Additional Information:© 1986 American Chemical Society. Received August 19, 1985; Revised Manuscript Received December 6, 1985. This research was supported by a grant from The National Science Foundation (DMB-8412754) and a grant-in-aid from the American Heart Association, California Affiliate, and with funds contributed by the American Heart Association Orange County Chapter. The 2H NMR experiments were performed at the Southern California Regional NMR Center (California Institute of Technology) supported by NSF Grant CHE79-16324. We thank Cecilia Kiang for much of the hygroscopic desorption work and April Diaz for help in the peptide synthesis work. Drs. Yesinowski and Chan of the Southern California Regional NMR Center (California Institute of Technology) provided valuable assistance in the ^2H NMR experiments.
Funders:
Funding AgencyGrant Number
NSFDMB-8412754
American Heart AssociationUNSPECIFIED
American Heart Association, Orange County ChapterUNSPECIFIED
NSFCHE79-16324
Issue or Number:9
Record Number:CaltechAUTHORS:20160516-132218945
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20160516-132218945
Official Citation:Mixtures of a series of homologous hydrophobic peptides with lipid bilayers: a simple model system for examining the protein-lipid interface Russell E. Jacobs and Stephen H. White Biochemistry 1986 25 (9), 2605-2612 DOI: 10.1021/bi00357a049
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:67136
Collection:CaltechAUTHORS
Deposited By: Ruth Sustaita
Deposited On:16 May 2016 21:44
Last Modified:03 Oct 2019 10:03

Repository Staff Only: item control page