Characterization of Paracetamol Binding with Normal and Glycated Human Serum Albumin Assayed by a New Electrochemical Method

In the present study the interactions between paracetamol (PC) and human serum albumin, in non-glycated (HSA) and glycated form (GHSA), were investigated using continuous cyclic voltammetry in acetate buffer pH 7.4. The results showed lack of significant changes in formal potential E-0 and electrode reaction constant rate, k(s), of PC. The decay in the drug current, after the addition of protein, showed a decrease in free drug concentration and formation of a biocomplex. The contentious coulometry was also used to determine the binding parameters. The binding constant and binding ratio for HSA and GHSA were 2.0x10(4) and 7.8x10(3) mol L-1, respectively, and the number of binding was 2:1 for HSA-PC and 1:1 for GHSA-PC. These results were confirmed by UV-Vis spectroscopy. Thus, the new electrochemical analysis method described here provides an easy and fast method for evaluation of drug-protein interactions with significant clinical implication in diabetes.