Acetylcholinesterase and carbonic anhydrase isoenzymes I and II inhibition profiles of taxifolin

Gocer H., Topal F., Topal M., KUCUK M., TEKE D., GÜLÇİN İ., ...Daha Fazla

JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, cilt.31, sa.3, ss.441-447, 2016 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 31 Sayı: 3
  • Basım Tarihi: 2016
  • Doi Numarası: 10.3109/14756366.2015.1036051
  • Dergi Adı: JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.441-447
  • Anahtar Kelimeler: Acetylcholinesterase, carbonic anhydrase, enzyme inhibition, enzyme purification, taxifolin, TROUT ONCORHYNCHUS-MYKISS, ANTIOXIDANT ACTIVITY, ISOFORMS-I, VITRO ANTIOXIDANT, CAFFEIC ACID, SULFONAMIDE DERIVATIVES, ANTIRADICAL ACTIVITIES, PHENOLIC-COMPOUNDS, ISOZYMES I, FLAVONOIDS
  • Atatürk Üniversitesi Adresli: Evet

Özet

Taxifolin, also known as dihydroquercetin, is a flavonoid commonly found in plants. Carbonic anhydrase (CA, EC 4.2.1.1) plays an important role in many critical physiological events including carbon dioxide (CO2)/bicarbonate (HCO3-) respiration and pH regulation. There are 16 known CA isoforms in humans, of which human hCA isoenzymes I and II (hCA I and II) are ubiquitous cytosolic isoforms. In this study, the inhibition properties of taxifolin against the slow cytosolic isoenzyme hCA I, and the ubiquitous and dominant rapid cytosolic isoenzyme hCA II were studied. Taxifolin, as a naturally bioactive flavonoid, has a K-i of 29.2nM against hCA I, and 24.2nM against hCA II. For acetylcholinesterase enzyme (AChE) inhibition, K-i parameter of taxifolin was determined to be 16.7nM. These results clearly show that taxifolin inhibited both CA isoenzymes and AChE at the nM levels.