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- W2051225816 abstract "X-ray photoelectron spectroscopy (XPS) has been used to characterize a poly(methyl methacrylate) (PMMA) surface with covalently attached proteins. The PMMA surfaces were first aminated using hexamethyldiamine; the resulting -NH(2) sites were reacted with the hetero-bifunctional cross-linker Sulfo-EMCS to form a maleimide-terminated surface. The N-hydroxysuccinimide ester terminal and maleimide terminal groups of Sulfo-EMCS reacts with amine and sulfhydryl groups, respectively, exposed on the surface of the proteins. This study characterizes Thermotoga maritima beta-glucosidase 1 (TmGH1), which belongs to a family of proteins that facilitate hydrolysis of glucose-related monomers with retention of conformation. The surfaces were characterized by XPS to monitor surface composition, and to elucidate protein orientation on the surface. Results suggest that a covalently bonded surface of TmGH1 on PMMA has been obtained. These results demonstrate the feasibility of using XPS to study protein surface chemistry and demonstrate a useful method to anchor cysteine-terminated proteins for the purposes of creating biosensors or platforms for mechanical force experiments to investigate protein structure." @default.
- W2051225816 created "2016-06-24" @default.
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- W2051225816 date "2010-06-01" @default.
- W2051225816 modified "2023-10-16" @default.
- W2051225816 title "Characterization of covalently bonded proteins on poly(methyl methacrylate) by X-ray photoelectron spectroscopy" @default.
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- W2051225816 doi "https://doi.org/10.1016/j.colsurfb.2010.02.012" @default.
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