Characterization of paracetamol binding with normal and glycated human serum albumin assayed by a new electrochemical method

Journal of the Brazilian Chemical Society

Parandis Daneshegar²  Ali Akbar Moosavi-movahedi²  Parviz Norouzi¹  Mohammad Reza Ganjali¹  Mohammad Farhadi¹  Nader Sheibanid¹ 

[1] ,University of Tehran Institute of Biochemistry & Biophysics Tehran,Iran

关键词: continuous cyclic voltammetry;    glycated human serum albumin;    paracetamol;    binding study;   

DOI  :  10.1590/S0103-50532012000200018

来源: SciELO

【 摘 要 】

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 E0 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 2.0×10(4) and 7.8×10³ 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.

【 授权许可】

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