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We propose a new way of regulating protein adsorption by using a p H-responsive polymer. According to the theoretical results obtained from the molecular theory and kinetic approaches, both thermodynamics and kinetics of protein adsorption are verified to be well controlled by the solution p H. The kinetics and the amount of adsorbed proteins at equilibrium are greatly increased when the solution environment changes from acid to neutral. The reason is that the increased p H promotes the dissociation of the weak polyelectrolyte, resulting in more charged monomers and more stretched chains.Thus the steric repulsion within the polymer layer is weakened, which effectively lowers the barrier felt by the protein during the process of adsorption. Interestingly, we also find that the kinetics of protein desorption is almost unchanged with the variation of p H. It is because although the barrier formed by the polymer layer changes along with the change of p H,the potential at contact with the surface varies equally. Our results may provide useful insights into controllable protein adsorption/desorption in practical applications.
We propose a new way of regulating protein adsorption by using ap H-responsive polymer. According to the theoretical results obtained from the molecular theory and kinetic approaches, both thermodynamics and kinetics of protein adsorption are verified. The kinetics and the amount of adsorbed proteins at equilibrium are greatly increased when the solution environment changes from acid to neutral. The reason is that the the increased p H promotes the dissociation of the weak polyelectrolyte, resulting in more charged monomers and more stretching chains. the steric repulsion within the polymer layer is weakened, which effectively lowers the barrier felt by the protein during the process of adsorption. Interestingly, we also find that the kinetics of protein desorption is almost unchanged with the variation of p H. It is because the barrier formed by the polymer layer changes along with the change of p H, the potential at contact with the s urface varies equally. Our results may provide insights into controllable protein adsorption / desorption in practical applications.