Kinetic investigation of protein adsorption into polyelectrolyte brushes by quartz crystal microbalance with dissipation: The implication of the chromatographic mechanism.

Kinetic investigation of protein adsorption into polyelectrolyte brushes by quartz crystal microbalance with dissipation: The implication of the chromatographic mechanism.
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通过石英晶体微天平耗散蛋白质吸附到聚电解质刷的动力学研究:色谱机制的含义。

DOI:
10.1016/j.chroma.2021.462460
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发表时间:
2021
影响因子:
4.1
通讯作者:
Qinghong Shi
Qinghong Shi
中科院分区:
化学2区
文献类型:
--
作者:
Fenfen You;Qinghong Shi

文献摘要

相似文献

With the growing concerns of polymer-grafted ion-exchange chromatography, the importance of protein adsorption on charged polymer-grafted surfaces cannot be stressed enough. However, a full understanding in adsorption in polymer brushes is still a great challenge due to the lack ofin situcharacterization technique. In this work, we use quartz crystal microbalance with dissipation toin situinvestigate adsorption kinetics of γ-globulin and recombinant human lactoferrin on poly(3-sulfopropyl methacrylate) (pSPM) sensors prepared via atom transfer radical polymerization. With an increase of chain length and grafting density, great increasing amounts of proteins onpSPM-grafted sensors revealed that protein underwent a transition from monolayer to multilayer adsorption. It was attributed to direct protein binding into charged brushes, in which more binding sites involved and more coupled water lost. However, such a strong binding and rigid structure of proteins limited the protein transport inpSPM brushes and “chain delivery” effect. With an increase in grafting density, moreover, denser brushes hindered adjustment in protein conformation inpSPM brushes and further exacerbated protein transport inpSPM brushes. Furthermore, the influence of buffer pH and salt concentration further validated the ion exchange characteristics of protein adsorption intopSPM brushes. The research provided a variety ofin situevidence of protein binding and conformation evolution inpSPM brushes and elucidated mechanism of protein adsorption inpSPM brushes.