We present a unique immobilization technique via physical adsorption/exchange of biomolecules onto a sensing surface of surface plasmon resonance (SPR). The adsorption/exchange is based on competitive bindings of biomolecules to a surface, which does not require a chemical modification of the biomolecules. SPR sensorgrams show that three human serum proteins, albumin, immunoglobulin G (IgG), and fibrinogen, have different adsorption strengths to the surface and the competitive adsorption of the individuals controls the exchange sequence. A target protein displaces a preadsorbed weak-affinity protein; however, a preadsorbed strong-affinity protein is not displaced by the target protein. In a microfluidic device, we engineer two gold surfaces covered by two known proteins. The sensor allows selective protein detection by being displaced by a target protein on only one of the surfaces. We demonstrate that IgG is selectively detected between albumin- and fibrinogen-adsorbed surfaces. Moreover, the physical adsorption without using an additional surface modification can lead to highly sensitive detection in SPR because of the exponential decay of surface plasmon resonance wave (SPW) from the sensing surface. Based on the competitive adsorption and exchange reaction, we may have a complementary detection system to existing complex and labor-intensive biomolecules detector by bypassing relying on bioreceptors and their attachment to the surface. The physisorbed interface may be useful for automated diagnostic systems. © 2010, Society for Laboratory Automation and Screening. All rights reserved.
Choi, S., & Chae, J. (2010). A Physisorbed Interface Design of Biomolecules for Selective and Sensitive Protein Detection. Journal of Laboratory Automation, 15(3), 172–178. https://doi.org/10.1016/j.jala.2009.09.002