Synthetic polypeptide adsorption to Cu-IDA containing lipid films: a model for protein-membrane interactions

Langmuir : the ACS Journal of Surfaces and Colloids
M S KentS Satija

Abstract

Adsorption of synthetic alanine-rich peptides to lipid monolayers was studied by X-ray and neutron reflectivity, grazing incidence X-ray diffraction (GIXD), and circular dichroic spectroscopy. The peptides contained histidine residues to drive adsorption to Langmuir monolayers of lipids with iminodiacetate headgroups loaded with Cu2+. Adsorption was found to be irreversible with respect to bulk peptide concentration. The peptides were partially helical in solution at room temperature, the temperature of the adsorption assays. Comparisons of the rate of binding and the structure of the adsorbed layer were made as a function of the number of histidines (from 0 to 2) and also as a function of the positioning of the histidines along the backbone. For peptides containing two histidines on the same side of the helical backbone, large differences were observed in the structure of the adsorbed layer as a function of the spacing of the histidines. With a spacing of 6 A, there was a substantial increase in helicity upon binding (from 17% to 31%), and the peptides adsorbed to a final density approaching that of a nearly completed monolayer of alpha-helices adsorbed side-on. The thickness of the adsorbed layer (17 +/- 2.5 A) was slightly g...Continue Reading

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Citations

Nov 18, 2009·Biophysical Journal·Chiu-Hao ChenMark L Schlossman
Apr 3, 2013·Current Protocols in Protein Science·John F AnknerDean A A Myles
Dec 16, 2010·Langmuir : the ACS Journal of Surfaces and Colloids·Jeanne C StachowiakDarryl Y Sasaki

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