Exploring the Inhibitory Effects of Quinolone Medications on Carbonic Anhydrase Enzyme Activity: In Vitro and In Silico Investigation

Abstract

AbstractEnzyme inhibition is a frequently employed technique for regulating enzyme activity in several biological systems that are physiologically significant. In this study, it was evaluated the effectiveness of six specific quinolone medicines, namely lomefloxacin, nalidixic acid, gatifloxacin, norfloxacin, sparfloxacin and nitrofurantoin, in inhibiting two human isoforms of the carbonic anhydrase (hCA) that play a role in different physiological and pathological circumstances. In order to achieve this objective, both in vitro and in silico investigations were conducted to get a deeper understanding of the potential binding interactions and affinities for hCA I and II isoforms. The kinetic inhibitory effects (Kis) of hCA I ranged from 1.31 to 13.07 μM, in comparison to the reference medication acetazolamide (AAZ, Ki of 0.12 μM). In addition, hCA II was effectively suppressed by these drugs, with Kis ranging from 1.42 to 11.93 μM, compared to AAZ (Ki of 0.098 μM). Significant interactions between the six medicines and hCAs indicated their potential to support therapeutic targets against pathological diseases. Furthermore, the findings acquired will contribute to the enhancement of therapeutic dose regimens for these medications and the prevention of unforeseen drug‐drug interactions when administered concurrently with other substances.