Oriented immobilization of antibodies with GST-fused multiple F c-specific B-domains on a gold surface

Tai Hwan Ha, Sun Ok Jung, Jeong Min Lee, Kun Yeong Lee, Yan Lee, Jong Sang Park, Bong Hyun Chung

Research output: Contribution to journalArticlepeer-review

56 Scopus citations


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 covalentiy tethered GBx proteins. A single antibody tethered on the GST-GB 3 is estimated to capture two antigens (enhanced green fluorescent protein), and this antigen capture ratio seems to be the most efficient value ever observed.

Original languageEnglish (US)
Pages (from-to)546-556
Number of pages11
JournalAnalytical chemistry
Issue number2
StatePublished - Jan 15 2007

Fingerprint Dive into the research topics of 'Oriented immobilization of antibodies with GST-fused multiple F <sub>c</sub>-specific B-domains on a gold surface'. Together they form a unique fingerprint.

Cite this