Electrochemical-spectroscopic-chemometric investigation of binding and inhibition of myeloperoxidase by bivalirudin: Application to determination of myeloperoxidase as a biomarker for acute coronary syndrome

In this paper, we are going to report results of one of our projects in which we have investigated binding and inhibition of myeloperoxidase (MO) by bivalirudin (BV) with the help of electrochemical and spectroscopic techniques assisted by chemometric methods. Different electrochemical and spectroscopic data were combined or individually used to justify binding and inhibition of the MO by BV. Hard and soft modeling chemometric methods were used to the analysis of experimental data to extract concentration profiles, pure instrumental signal profiles and binding constant value (Kb). Results of conventional and chemometric analyses confirmed a relatively strong binding of BV with MO which inhibited it. Concentration and pure instrumental signal profiles revealed interaction and binding of BV with MO and formation of one complex species. Inhibition of the MO by BV helped us to exploit a quantitative concept for electrochemical determination of the MO based on its binding with BV. Determination of the MO was performed by electrochemical impedance spectroscopy (EIS) and differential pulse voltammetry (DPV) and the results of the EIS were better than DPV which can be suggested for the analysis of serum samples with the aim of evaluation of patients with acute coronary syndrome.

Automated summary

This paper reports the results of a project which investigated the binding and inhibition of MO by BV using electrochemical and spectroscopic techniques assisted by chemometric methods. The analyses confirmed strong binding of BV with MO and proposed a quantitative concept for electrochemical determination of MO based on its binding with BV. The EIS results were suggested as more effective than DPV for analyzing serum samples in evaluating patients with acute coronary syndrome.