The Relative Diffusivities of Bound and Unbound Protein Can Control Chemotactic Directionality

Abstract: Enzyme-based systems have been shown to undergo directional motion in response to their substrate gradient. Here, we formulate a kinetic model to analyze the directional movement of an ensemble of protein molecules in response to a gradient of the ligand. A similar analysis has been performed to probe the motion of enzyme molecules in response to a gradient of the substrate under catalytic conditions. In both cases, a net movement up the ligand/substrate gradient is predicted when the diffusivity of the ligand/substrate-bound protein is lower than that of the unbound protein (positive chemotaxis). Conversely, movement down the ligand/substrate gradient is expected when the diffusivity of the ligand/substrate-bound protein is higher than that of the unbound protein (negative chemotaxis). The work underscores the critical importance of measuring the diffusivity of the bound protein and compare it with that of the free protein.