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Updated: Aug 8, 2026

Biomembrane Fabrication by the Solvent-assisted Lipid Bilayer (SALB) Method
Published on: December 1, 2015
Glycophorin-induced cholesterol-phospholipid domains in dimyristoylphosphatidylcholine bilayer vesicles
R Tampé1, A von Lukas, H J Galla
1Institute of Biochemistry, Technical University Darmstadt, FRG.
Abstract:
Glycophorin has been incorporated into unilamellar cholesterol-containing dimyristoylphosphatidylcholine vesicles that were reconstituted by the freeze and thaw technique. Evidence was obtained for a protein-induced structural reorganization of these mixed membranes. By differential scanning calorimetry, we were able to construct a phase diagram for the phospholipid/cholesterol mixture consisting of a liquid-ordered, a solid-ordered, and a liquid-disordered phase. Glycophorin at low molar fractions (XG less than 3 X 10(-3)) increases the relative amount of lipid in the liquid-ordered phase, which is interpreted as an enrichment of cholesterol in the vicinity of the protein. The formation of such steroid-enriched domains could be demonstrated directly by electron paramagnetic resonance using a spin-labeled cholesterol analogue. A drastic increase of the spin-spin interaction of the labeled steroid was observed in the presence of glycophorin.
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