Membrane domain formation induced by binding/unbinding of curvature-inducing molecules onto both membrane surfaces

Abstract: The domain formation of curvature-inducing molecules, such as peripheral or transmembrane proteins and conical surfactants, is studied in thermal equilibrium and nonequilibrium steady states using meshless membrane simulations. These molecules can bind onto both surfaces of a bilayer membrane and also move to the opposite leaflet by a flip-flop. In symmetric conditions for the two leaflets, the membrane domains form checkerboard patterns in addition to stripe and spot patterns. The unbound membrane stabilizes the vertices of the checkerboard. In asymmetric conditions, the domains form kagome-lattice and thread-like domains. In the nonequilibrium steady states, a flow of the binding molecules between the upper and lower solutions can occur via the flip-flop.