Adsorption of Protein on Hydrophobin Surface Driven by Electrostatic Force

Abstract

Abstract: Hydrophobins are small secreted proteins produced by filamentous fungi, which can form an amphipathic membrane at various surfaces. Hydrophobins have been considered as excellent substrates for protein immobilization. However, the driven force for protein adsorption on hydrophobin surface is not clear. In this work, we systematically investigated the protein adsorption on hydrophobins at different pH and ionic strength. Firstly, the adsorption of class Ⅰ hydrophobin HGFI and class Ⅱ hydrophobin HFBI on the surfaces of polystyrene were investigated via quartz crystal microbalance with dissipation monitoring(QCM-D) at different pH and ionic strength. The results show that both pH and ionic strength have greater impacts on the adsorption of HGFI on polystyrene than that of HFBI. Moreover, HGFI can form soft films on the polystyrene, whereas HFBI formed very rigid films under the same conditions. The adsorption of BSA and avidin on the HGFI and HFBI were further investigated by using QCM-D at the same pH and ionic strength. The results indicate that adsorptions of BSA and avidin on the HGFI and HFBI are dramatically affected by both pH and ionic strength, suggesting that the major driving force dominating the protein adsorption on hydrophobin is the electrostatic force. This study provides a theoretical guide for a controllable immobilization of a protein on a hydrophobin surface.

Key words: Hydrophobin, Soft film, Rigid film, Electrostatic force, Quartz crystal microbalance

TrendMD:

WANG Ze-Fang, HUANG Yu-Jian, NIU Bao-Long, LI Shan, WANG Dan-Dan, XU Hai-Jin, QIAO Ming-Qiang*. Adsorption of Protein on Hydrophobin Surface Driven by Electrostatic Force[J]. Chem. J. Chinese Universities, 2010, 31(10): 2052.

References

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