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Esterase activity and interaction of human hemoglobin with diclofenac sodium: A spectroscopic and molecular docking study
Author(s) -
Dohare Neeraj,
Siddiquee Md. Abrar,
Parray Mehrajud din,
Kumar Amit,
Patel Rajan
Publication year - 2020
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.2841
Subject(s) - chemistry , diclofenac sodium , circular dichroism , hemoglobin , gibbs free energy , fluorescence , förster resonance energy transfer , esterase , docking (animal) , fluorescence spectroscopy , enthalpy , biophysics , biochemistry , enzyme , chromatography , thermodynamics , medicine , physics , nursing , quantum mechanics , biology
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.