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Examines NSAIDs' interactions with BSA and DNA using spectral and electrochemical methods, indicating potential implications for drug design.
The role of two different non‐steroidal anti‐inflammatory drugs, namely, mefenamic acid (MA) (2‐[(2,3‐dimethylphenyl)amino]benzoic acid) and aceclofenac (ACF) (2‐[(2,6‐dichlorophenyl)amino]phenyl acetoxyacetic acid), and their electrostatic interactions with bovine serum albumin (BSA) and adenine model systems have been studied. The binding affinity for drug formation depends primarily on the heterocyclic ring and functional groups. The hydrophobic interactions were also evaluated. The spectral properties of the interactions were investigated by UV–visible, fluorescence, FT‐IR, cyclic voltammetry and molecular modelling methods. In addition, the Stern–Volmer plots for BSA and adenine with the drug molecules are shown. Moreover, the static quenching interaction, the binding constant ( K a ) and the number of sites ( n ) have been determined. The binding efficiency is evaluated and compared on the basis of its E value. The free energy, van der Waals and hydrogen‐bonding interaction values of BSA with the drugs are determined. In order to assess the electrochemical process, the scan rate is another important parameter, which has been determined by using cyclic voltammograms.
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Thulasidhasan et al. (2026) studied this question.
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