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Esterase activity and interaction of human hemoglobin with diclofenac sodium: A spectroscopic and molecular docking
Neeraj Dohare1, Md Abrar Siddiquee1, Mehrajud Din Parray1
1Biophysical Chemistry Laboratory, Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, India.
Abstract:
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.
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