Abstract
Cell membranes control structure and function through self–assembly by manipulating the interactions between diverse molecules. Since the kinetics and thermodynamics are governed by the chemical and physical conditions of the reaction fields, many studies have been conducted using well plates, petri dishes, and test tubes as reaction vessels to study the interactions between cell membranes and proteins under various compositions, temperatures, and concentrations. However, one of the major differences between such experimental conditions in the laboratory and those in living systems is that most of the former studies are conducted in closed systems, whereas living systems govern the kinetics and thermodynamics of various self–organizations under essentially open systems. In this paper, we will attempt to discuss the differences in protein self–assembly at the cell membrane interface in closed and open systems from calculations and experiments, using the self–assembly of amyloid–, the protein responsible for Alzheimer’s disease.
