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Issue 14, 2011
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Effects of surface curvature and surface chemistry on the structure and activity of proteins adsorbed in nanopores

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Abstract

The interactions of proteins with the surface of cylindrical nanopores are systematically investigated to elucidate how surface curvature and surface chemistry affect the conformation and activity of confined proteins in an aqueous, buffered environment. Two globular proteins, lysozyme and myoglobin, with different catalytic functions, were used as model proteins to analyze structural changes in proteins after adsorption on ordered mesoporous silica SBA-15 and propyl-functionalized SBA-15 (C3SBA-15) with carefully controlled pore size. Liquid phase ATR-FTIR spectroscopy was used to study the amide I and II bands of the adsorbed proteins. The amide I bands showed that the secondary structures of free and adsorbed protein molecules differ, and that the secondary structure of the adsorbed protein is influenced by the local geometry as well as by the surface chemistry of the nanopores. The conformation of the adsorbed proteins inside the nanopores of SBA-15 and C3SBA-15 is strongly correlated with the local geometry and the surface properties of the nanoporous materials, which results in different catalytic activities. Adsorption by electrostatic interaction of proteins in nanopores of an optimal size provides a favorably confining and protecting environment, which may lead to considerably enhanced structural stability and catalytic activity.

Graphical abstract: Effects of surface curvature and surface chemistry on the structure and activity of proteins adsorbed in nanopores

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Publication details

The article was received on 26 Oct 2010, accepted on 14 Feb 2011 and first published on 02 Mar 2011


Article type: Paper
DOI: 10.1039/C0CP02273J
Citation: Phys. Chem. Chem. Phys., 2011,13, 6689-6698
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    Effects of surface curvature and surface chemistry on the structure and activity of proteins adsorbed in nanopores

    L. Sang and M. Coppens, Phys. Chem. Chem. Phys., 2011, 13, 6689
    DOI: 10.1039/C0CP02273J

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