Carbonic anhydrase inhibitors: in vitro inhibition of alpha isoforms (hCA I, hCA II, bCA III, hCA IV) by flavonoids
JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, cilt.28, sa.2, ss.283-288, 2013 (SCI-Expanded, Scopus)
- Yayın Türü: Makale / Tam Makale
- Cilt numarası: 28 Sayı: 2
- Basım Tarihi: 2013
- Doi Numarası: 10.3109/14756366.2011.643303
- Dergi Adı: JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
- Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
- Sayfa Sayıları: ss.283-288
- Anahtar Kelimeler: Carbonic anhydrase, flavonoid, inhibitor, phenol, ACTIVE-SITE, PURIFICATION, COUMARINS, ISOZYMES, BINDING
- Ondokuz Mayıs Üniversitesi Adresli: Evet
Özet
A series of flavonoids, such as quercetin, catechin, apigenin, luteolin, morin, were investigated for their inhibitory effects against the metalloenzyme carbonic anhydrase (CA). The compounds were tested against four alpha-CA isozymes purified from human and bovine (hCA I, hCA II, bCA III, hCA IV) tissues. The four isozymes showed quite diverse inhibition profiles with these compounds. The flavonoids inhibited hCA I with K-I-s in the range of 2.2-12.8 mu M, hCA II with K-I-s in the range of 0.74-6.2 mu M, bCA III with K-I-s in the range of 2.2-21.3 mu M, and hCA IV with inhibition constants in the range of 4.4-15.7, with an esterase assay using 4-nitrophenyl acetate as substrate. Some simple phenols/sulfonamides were also investigated as standard inhibitors. The flavonoids incorporate phenol moieties which inhibit these CAs through a diverse, not yet determined inhibition mechanism, compared to classic inhibitors such as the sulfonamide/sulfamate ones.