Esterase activity and interaction of human hemoglobin with diclofenac sodium: A spectroscopic and molecular docking study

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.

A biophysical approach to study the impact of muscle relaxant drug tizanidine on stability and activity of serum albumins

“…Similar results were obtained by Rabbani et al, where an increase in the α‐helical content of HSA was seen in its interaction with the muscle relaxant drug eperisone hydrochloride from 48 to 59% 10 . These results suggest that the binding of TND with BSA and HSA is due to the dense conformation over the polypeptide backbone and the hydrophobic voids get hidden, which disrupts its microstructure 1 …”

“…The interaction of proteins with drugs has a vital role in the adsorption, distribution, metabolism, and transportation of various drugs 1 . The interaction of drugs with serum proteins has a strong impact on the pharmacodynamics and pharmacokinetics of drugs as well as on the structural and physiological activity of the carrier proteins 2 .…”

“…Esterase activity of BSA/HSAEsterase activity was employed to monitor the effect of the drug on the catalytic activity of BSA/HSA at various concentrations of substrate, PNPA (para-nitrophenyl acetate). The BSA/HSA assay was observed at individual concentrations of PNPA in the absence and presence of the drug by noticing the absorbance of the new product (p-nitrophenol) at a fixed wavelength of 405 nm 1. For each concentration of the substrate, the absorbance was recorded and fitted correspondingly to the Michaelis-Menten equation and Lineweaver-BurkF I G U R E 7 Synchronous fluorescence spectra of HSA as a function of TND concentration A, Δλ = 15 nm; B, Δλ = 60 nm, (T = 298 K, pH = 7.4).…”

Recognition of human hemoglobin with macromolecularly imprinted polymeric nanoparticles using non‐covalent interactions

“…Dohare et al also reported similar type of results showing that hydrogen bonds play an important role in the interactions between the nonsteroidal anti‐inflammatory drug (DIC) and hemoglobin 53 . In another study, couplings based on both hydrophobic interactions and hydrogen bonds between docetaxel (DTX) and human hemoglobin (HHb) have been proven 54 .…”

In vitro interactions of esculin and esculetin with bovine hemoglobin alter its structure and inhibit aggregation: insights from spectroscopic and computational studies

“…5 This interaction between proteins and small ligands can provide substantial structural and mechanical data for aiding drug discovery development. [6][7][8] Hemoglobin (Hb), an Fe(II) containing polypeptide, is a tetrameric globular protein comprising two ab dimers. 9 An individual a chain is made up of 141 amino acid residues forming seven helices and a b chain is made up of 146 amino acids forming eight helices.…”