期刊
COLLOIDS AND SURFACES B-BIOINTERFACES
卷 109, 期 -, 页码 115-120出版社
ELSEVIER
DOI: 10.1016/j.colsurfb.2013.03.033
关键词
Protein conformation; Protein unfolding; Graphene oxide; Glucose oxidase
资金
- National Natural Science Foundation of China [21175067, 21273117]
- Research Fund for the Doctoral Program of Higher Education of China [20103207110004]
- Natural Science Foundation of Jiangsu Province, China [BK2011779]
- Foundation of the Jiangsu Education Committee [09KJA150001, 10KJB150009, 10KJD150007]
- Program for Outstanding Innovation Research Team of Universities in Jiangsu Province, China
- Priority Academic Program Development of Jiangsu Higher Education Institutions, China
The adsorption of proteins on the surface of nanomaterials can induce changes in the structure and biological activity of the proteins. Although there have been a number of studies aimed at developing an understanding of the interactions of proteins with surfaces of nanomaterials, a detailed description of the actual state of the adsorbed proteins or the functional consequences of protein adsorption onto nanomaterials has yet to be reported. In this study, the conformation changes of glucose oxidase (GOx) induced by adsorption on graphene oxide (GO) sheets were investigated by quantitative second-derivative infrared analysis and two-dimensional infrared correlation spectroscopy (2D IR). The adsorption of GOx on GO sheets resulted in the conversion of alpha-helix to beta-sheet structures and therefore led to substantial conformation changes of GOx, even the unfolding of the protein. These alterations in the conformation of GOx caused a significant decrease in the catalytic activity of the enzyme for glucose oxidation. This study demonstrates that nanomaterials can strongly influence the conformation and activity of adsorbed proteins. In addition to the importance of this effect in cases of the direct adsorption of proteins on nanomaterials, the results have implications for proteins adsorbed on materials with nanometer-scale surface roughness. (C) 2013 Elsevier B.V. All rights reserved.
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