+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

Mixtures of a series of homologous hydrophobic peptides with lipid bilayers: a simple model system for examining the protein-lipid interface

Mixtures of a series of homologous hydrophobic peptides with lipid bilayers: a simple model system for examining the protein-lipid interface

Biochemistry 25(9): 2605-2612

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.

Please choose payment method:

(PDF emailed within 0-6 h: $19.90)

Accession: 040710630

Download citation: RISBibTeXText

PMID: 3718968

DOI: 10.1021/bi00357a049

Related references

Semisynthetic Proteins: Model Systems for the Study of the Insertion of Hydrophobic Peptides into Preformed Lipid Bilayers. Biochemistry 33(51): 15469-15482, 1994

Direct observation of lipid domains in free standing bilayers: From simple to complex lipid mixtures. Chemistry and Physics of Lipids 122(1-2): 137-145, 2003

Direct AFM observation of saposin C-induced membrane domains in lipid bilayers: from simple to complex lipid mixtures. Chemistry and Physics of Lipids 132(1): 15-22, 2004

Binding of cationic model peptides (KX) 4 K to anionic lipid bilayers: Lipid headgroup size influences secondary structure of bound peptides. Biochimica et Biophysica Acta. Biomembranes 1859(3): 415-424, 2017

Molecular dynamics simulations of model trans-membrane peptides in lipid bilayers: a systematic investigation of hydrophobic mismatch. Biophysical Journal 90(7): 2326-2343, 2006

Phase diagram and lipid selectivity of lipid-protein bilayers with hydrophobic mismatch. Biophysical Journal 64(2 Part 2): A15, 1993

Apolipoprotein A-II and Serum High-Density Lipoproteins: A Model System for the Study of Protein-Lipid Interactions at a Natural Hydrophilic-Hydrophobic Interface. Biophysical Journal 37(1): 179-181, 1982

Interfacial adsorption of simple lipid mixtures combined with hydrophobic surfactant protein from pig lung. Biochemistry and Cell Biology 70(5): 332-338, 1992

Interfacial interactions of hydrophobic peptides with lipid bilayers. Journal of Colloid and Interface Science 246(1): 60-69, 2002

The interaction of small hydrophobic peptides with lipid bilayers. Biophysical Journal 47(2 Part 2): 174A, 1985

The effect of charge on permeation of hydrophobic peptides across lipid bilayers. Pharmaceutical Research (New York) 14(11 Suppl. ): S152, 1997

Probing the interaction forces between hydrophobic peptides and supported lipid bilayers using AFM. Journal of Molecular Recognition 20(6): 538-545, 2007

Interactions of hydrophobic peptides with lipid bilayers: Monte Carlo simulations with M2delta. Biophysical Journal 85(6): 3431-3444, 2003

Hydrophobic mismatch and the incorporation of peptides into lipid bilayers: a possible mechanism for retention in the Golgi. Biochemistry 37(2): 673-679, 1998

Interactions of cationic-hydrophobic peptides with lipid bilayers: a Monte Carlo simulation method. Biophysical Journal 93(6): 1858-1871, 2007