Kinetics of protein adsorption/desorption mediated by pH-responsive polymer layer  

作　　者：苏晓航 雷群利 任春来 

机构地区：[1]National Laboratory of Solid State Microstructures and Department of Physics,Nanjing University

出　　处：《Chinese Physics B》2015年第11期231-237,共7页中国物理B（英文版）

基　　金：supported by the National Natural Science Foundation of China(Grant Nos.21274062,11474155,and 91027040)

摘　　要：We propose a new way of regulating protein adsorption by using a pH-responsive polymer. According to the the- oretical 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 pH. The kinetics and the amount of adsorbed proteins at equi- librium are greatly increased when the solution environment changes from acid to neutral. The reason is that the increased pH 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 pH. It is because although the barrier formed by the polymer layer changes along with the change of pH, 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 a pH-responsive polymer. According to the the- oretical 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 pH. The kinetics and the amount of adsorbed proteins at equi- librium are greatly increased when the solution environment changes from acid to neutral. The reason is that the increased pH 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 pH. It is because although the barrier formed by the polymer layer changes along with the change of pH, the potential at contact with the surface varies equally. Our results may provide useful insights into controllable protein adsorption/desorption in practical applications.

关 键 词：DISSOCIATION potential of mean-force BARRIER steric repulsion 

分 类 号：O647.3[理学—物理化学]