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Thermally induced shape fluctuations of giant quasi/spherical lipid vesicles are used to study the bending elasticity modulus kc of a phospholipid (PHLP) membranes in presence of beta 2 glycoprotein I (β2/GPI) in the aqueous solution which surrounds the vesicle's membrane. The bending elastic modulus kc of PHLP - protein membrane was obtained for different mass concentrations of β2/GPI for pure neutral SOPC membranes and for mixed SOPC: Cardiolipin negatively charged membranes. The experimental results for the bending elastic modulus kc of the PHLP membranes does not show dependence on the concentration of β2/GPI in the range from 5.5 to 55 >g/ml, when β2/GPI is present in the aqueous solution surrounding the vesicle's membrane. Obtained results are in good agreement with predictions, based on different experiments, explaining the mechanism of binding of β2/GPI to neutral membranes.

Bending elasticity of lipid membranes in presence of beta 2 glycoprotein I in the surrounding solution