PMID: 9168142Apr 26, 1997Paper

Time-resolved X-ray reflectivity measurements of protein binding onto model lipid membranes at the air-water interface

Biochimica Et Biophysica Acta
U Vierl, G Cevc

Abstract

The energy-dispersive X-ray reflectometry and turbidity measurements are used to investigate the kinetics of concanavalin A binding onto the distearoylphosphatidylcholine/distearoylphosphatidylethanolamine-+ ++maltobionamide (DSPC/DSPE-mal1) or distearoylphosphatidylcholine/distearoylphosphatidylethanolamine-+ ++maltotetrabionamide (DSPC/mal3) mixed monolayer at the air-water interface. The resulting adsorbed layer of this sugar-binding protein near the membrane with one or three hexoses in the lipid head-group is 3.9 nm or 9.7 nm thick, respectively. The different thicknesses of the adsorbed layer can be correlated with the diverse orientations of the adsorbed proteins. These lay flat on the surface containing DSPE-mal1 and 'perpendicular' to the surface containing DSPE-mal3. The monolayer structure is little affected by concanavalin A binding, but the incorporation of sugar lipids decreases the chain tilt and the interfacial thickness marginally. The binding is quasi-exponential with the time constant between some minutes and several hours depending on the concanavalin A and vesicle concentrations in the bulk. The experimental resolution of the time-resolved measurements made with the laboratory-based instrument is 15 min and...Continue Reading

Citations

Jan 12, 2005·Biochemistry·Colin P JohnsonDeborah E Leckband
Aug 29, 2009·Langmuir : the ACS Journal of Surfaces and Colloids·Clare M HollinsheadM Jayne Lawrence

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