Influence of ionic strength and beta2-glycoprotein I concentration on agglutination of like-charged phospholipid membranes

• We studied the adhesion between like-charged vesicles experimentally and theoretically.
• In a Monte Carlo model we observed the orientation of the beta-2 GPI near charged surface.
• We observed beta-2 GPI electrostatic based adhesion on a charged membrane.
• Ionic strength of salt solution decreases the adhesion between charged vesicles.

The effect of ionic strength on adhesion between negatively charged giant unilamellar vesicles induced by beta2-glycoprotein I (β2-GPI) was studied experimentally and theoretically. Measuring the effective angle of contact between adhering vesicles indicated that the strength of adhesion between vesicles decreases with increasing ionic strength, and increases with concentration of β2-GPI. In the theoretical part we focused on the study of the average orientation of β2-GPI near the charged membrane and its role in mediating the attractive interactions between the vesicles. β2-GPI proteins were modelled as rods with internal distribution of electric charge. The predictions of Monte Carlo simulations show orthogonal orientation of some of the membrane attached β2-GPI in narrow gap between two vesicles. On the contrary, at larger distances between vesicles the proteins are parallelly attached to the membrane surface. A local minimum of the free energy corresponding to β2-GPI-mediated adhesion of two neighbouring vesicles was predicted. The strength of adhesion was confirmed to decrease at high ionic strength.

Figure optionsDownload as PowerPoint slide