Abstract

The kinetic behavior of glutathione (GSH)/ glutathione-S-transferase (GST) was investigated using surface plasmon resonance (SPR). Here, an alkanethiol-modified chip incorporated with bovine serum albumin (BSA) was employed. Subsequently, GSH was anchored on BSA surface only in the experimental channel and the without-active BSA surface was designed as the reference channel to improve the quality of the binding data and prevent a number of experimental artifacts to complicate the final biosensor analysis. Our results demonstrated that the BSA-modified chip was effective not only in binding the target proteins but also in suppressing the nonspecific binding (NSB) of proteins.

Key words: Surface plasmon resonance, bovine serum albumin, glutathione, glutathione-S-transferase, alkanethiol.

Abbreviation

GSH, glutathione; GST, glutathione-S-trans- ferase; SPR, surface plasmon resonance; NSB, nonspecific binding; BSA, bovine serum albumin;SAMs, self-assembled monolayers; PDEA, 2-(2-pyridinyldithio) ethane amine hydro- chloride; BS³, Bis(3-sulfo-N-hydroxysuccinimide ester) sodium salt; GMBS,suberic acid 4-maleimidobutyric acid N-hydro- xysuccinimide ester; PBS,phosphate buffered saline tablets; DMSO, dimethylsulfoxide; EDC, 1-ethyl-3-[3- dimethylamino- propyl]carbodiimide hydrochloride; NHS, N-hydroxysuccini- mide.