Esterase activity and interaction of human hemoglobin with diclofenac sodium: A spectroscopic and molecular docking study.
J Mol Recognit. 2020 Mar 09;:e2841
Authors: Dohare N, Siddiquee MA, Parray MD, Kumar A, Patel R
To get an idea about the pharmacokinetics and pharmacodynamics, it is important to study the drug-protein interaction. Therefore, herein, we studied the interaction of diclofenac sodium (DIC) with human hemoglobin. The binding study of nonsteroidal antiinflammatory drug, DIC with human hemoglobin (HHB) was done by utilizing fluorescence, UV-visible, time-resolved fluorescence and far-UV circular dichroism spectroscopy (CD). Various thermodynamic parameters such as enthalpy change (ΔH), entropy change (ΔS), and Gibbs free energy change (ΔG) were also calculated. CD results showed that DIC induces secondary structure change in HHB. Fluorescence resonance energy transfer was also performed. Additionally, it was also observed that DIC inhibits the esterase-like enzymatic activity of HHB via competitive inhibition.
PMID: 32150309 [PubMed - as supplied by publisher]