Esterase activity and interaction of human hemoglobin with diclofenac sodium: A spectroscopic and molecular docking study. Issue 8 (9th March 2020)

• Record Type: Journal Article
• Authors: Dohare, Neeraj; Siddiquee, Md. Abrar; Parray, Mehrajud din; Kumar, Amit; Patel, Rajan
• Is Part Of: Journal of molecular recognition. Volume 33:Issue 8(2020)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2020-03-09
• Subjects: diclofenac sodium -- esterase activity -- human hemoglobin -- quenching -- time‐resolved fluorescence; Molecular recognition -- Periodicals; Models, Molecular -- Periodicals; Molecular Conformation -- Periodicals; Molecular Sequence Data -- Periodicals; Molecular Structure -- Periodicals; Carrier Proteins -- Periodicals; 572.8
• DOI: 10.1002/jmr.2841
• Languages: English
• ISSNs: 0952-3499

Abstract

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. Abstract : Graphical representation of the interaction between human hemoglobin and diclofenac sodium.