Abstract
Surface plasmon resonance (SPR) biosensing provides a powerful tool for label-free kinetic analysis of antibody-antigen interactions. SPR analysis can be improved with biosensing interfaces based on graphene oxide (GO), which will enhance the accuracy of determination of kinetic constants and expand a range of suitable targets. GO possesses large surface area and oxygen-containing functional groups for covalent immobilization of biomolecules. Here, we are proposing an SPR biosensing interface based on a GO linking layer with immobilized protein A, which allows orientation-specific immobilization of antibodies. Protein A was covalently attached to the surface of GO via amine coupling. Thereafter, the developed biosensing interface was used for the analysis of the interaction between anti-bovine serum albumin (BSA) antibody and BSA.
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