Interaction of carbonic anhydrase isozymes I and II with antibiotic agent gatifloxacin
5th International Eurasian Conference on Biological and Chemical Sciences (EurasianBioChem 2022), Ankara, Türkiye, 23 - 25 Kasım 2022, ss.299, (Özet Bildiri)
- Yayın Türü: Bildiri / Özet Bildiri
- Basıldığı Şehir: Ankara
- Basıldığı Ülke: Türkiye
- Sayfa Sayıları: ss.299
- Erzincan Binali Yıldırım Üniversitesi Adresli: Evet
Özet
Metalloenzyme inhibition is a widely used technique for managing enzymatic activity in diverse biological systems with
physiological relevance. The reversible hydration of carbon dioxide to bicarbonate and proton is catalyzed by carbonic
anhydrases (CAs), known as metalloenzymes. Only twelve humans (h) isoenzymes are catalytically active and involved
in significant activities, including pH balance, bone resorption, calcification, electrolyte secretions, gluconeogenesis,
respiration, and tumorigenesis. In this study, the cytosolic isoform hCA I, which is distributed widely in erythrocytes and
the gastrointestinal (GI) tract, was low-level inhibited by gatifloxacin, which is a fourth-generation fluoroquinolone, at
micromolar concentration with KI of 13.07 ± 0.92 µM compared with the reference drug acetazolamide (AAZ, KI of 0.19
± 0.01 µM). In the same direction, another isoform, hCA II, found mainly in the GI tract, eyes, kidney, bone osteoclasts,
brain, lungs, erythrocytes, and testis, was also a weakly inhibited isoform by this drug, with KI of 11.93 ± 1.14 µM
compared with AAZ (KI of 0.17 ± 0.01 µM). Additionally, the active sites of the hCA I and II isoforms were investigated
using molecular docking experiments to determine the likely binding interactions and affinities for the gatifloxacin.