The binding constant of membraneanchored receptors and ligands depends strongly on the nanoscale roughness of the membranes

Jun 27, 2013 | 04:00 PM

Location

Dr. Thomas Weikl, Max Planck Institute of Colloids and Interfaces, Potsdam Department of Theory and Bio-Systems

Cell adhesion and the adhesion of vesicles to the membranes of cells or organelles are pivotal for immune responses, tissue formation, and cell signaling. The adhesion processes depend sensitively on the binding constant of the membrane-anchored receptor and ligand proteins that mediate adhesion, but this constant is difficult to measure in experiments. We have investigated the binding of membrane-anchored receptor and ligand proteins with molecular dynamics simulations. We find that the binding constant of the anchored proteins strongly decreases with the membrane roughness caused by thermally excited membrane shape fluctuations on nanoscales. We present a theory that explains the roughness dependence of the binding constant for the anchored proteins from membrane confinement and provides a general relation to the binding constant of soluble proteins without membrane anchors. Since the binding constant of soluble proteins is readily accessible in experiments, our results provide a novel route to compute the binding constant of membraneanchored receptor and ligand proteins.

Time & Location

Jun 27, 2013 | 04:00 PM

Seminar Room T2 (1.4.03)