Investigation of Ph-Assisted Human Serum Albumin (HSA)-Cobalt (Co)Binding Using Nanomechanical Deflection and Circular Dichroism

Abstract

Human serum albumin (HSA)-cobalt (Co) binding assay could serve as a marker for early detection of myocardial ischemia. However, the binding mechanism of the HSA-Co assay is very complex and hard to detect. During myocardial ischemia, the physiological pH may change with subsequent decrease in binding of Co with HSA. In this paper, we have investigated the binding of Co with HSA functionalized on the surface of microcantilever at acidic, basic and neutral pHs. Conformational change of HSA upon injection of Co(II) ions resulted in deflection of cantilever sensors. Furthermore, spectroscopic insight was obtained using circular dichroism to analyze conformational change of HSA-Co(II) binding.