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• W1978327447 endingPage "556" @default.
• W1978327447 startingPage "546" @default.
• W1978327447 abstract "We have constructed a novel platform for the oriented buildup of immunoglobulins on a gold surface for a surface plasmon resonance imaging microarray. To this end, genetically engineered glutathione S-transferase proteins bearing one, two, and three Fc-specific B-domains in protein G from Streptococci (GST-GB1, -GB2, and -GB3, respectively) were produced. In order to tether these GST-GBx proteins specifically, a novel glutathione-derivatized ligand (LA-GSH) was also synthesized from a biaminated tri(ethylene glycol) backbone. Each end of the backbone was further functionalized with a maleimide group for a glutathione modification and a lipoic acid for surface immobilization. The glutathione ligand demonstrated a negligible nonspecific protein adsorption toward other spectator proteins while showing a strong specific association toward GST-GBx proteins. This Fc-specific surface exhibited at least a 2-fold enhancement in the immunoglobulin density (from human and mouse) with its antigen capture capability totally conserved compared to a covalently tethered GBx proteins. A single antibody tethered on the GST-GB3 is estimated to capture two antigens (enhanced green fluorescent protein), and this antigen capture ratio seems to be the most efficient value ever observed." @default.
• W1978327447 created "2016-06-24" @default.
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• W1978327447 date "2006-11-16" @default.
• W1978327447 modified "2023-09-27" @default.
• W1978327447 title "Oriented Immobilization of Antibodies with GST-Fused Multiple F_c-Specific B-Domains on a Gold Surface" @default.
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• W1978327447 doi "https://doi.org/10.1021/ac061639+" @default.
• W1978327447 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17222019" @default.
• W1978327447 hasPublicationYear "2006" @default.
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