Capsaicin: A Potent Inhibitor of Carbonic Anhydrase Isoenzymes

ARABACI B., GÜLÇİN İ., Alwasel S.

MOLECULES, cilt.19, sa.7, ss.10103-10114, 2014 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 19 Sayı: 7
  • Basım Tarihi: 2014
  • Doi Numarası: 10.3390/molecules190710103
  • Dergi Adı: MOLECULES
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.10103-10114
  • Anahtar Kelimeler: capsaicin, carbonic anhydrase, enzyme purification, enzyme inhibition, affinity chromatography, TROUT ONCORHYNCHUS-MYKISS, ERYTHROCYTES IN-VITRO, ISOFORMS-I, ISOZYMES I, SULFONAMIDE DERIVATIVES, ANTIOXIDANT PROPERTIES, RED-PEPPER, METABOLISM, SERIES, (3,4-DIHYDROXYPHENYL)(2,3,4-TRIHYDROXYPHENYL)METHANONE
  • Atatürk Üniversitesi Adresli: Evet

Özet

Carbonic anhydrase (CA, EC 4.2.1.1) is a zinc containing metalloenzyme that catalyzes the rapid and reversible conversion of carbon dioxide (CO2) and water (H2O) into a proton (H+) and bicarbonate (HCO3-) ion. On the other hand, capsaicin is the main component in hot chili peppers and is used extensively used in spices, food additives and drugs; it is responsible for their spicy flavor and pungent taste. There are sixteen known CA isoforms in humans. Human CA isoenzymes I, and II (hCA I and hCA II) are ubiquitous cytosolic isoforms. In this study, the inhibition properties of capsaicin against the slow cytosolic isoform hCA I, and the ubiquitous and dominant rapid cytosolic isozymes hCA II were studied. Both CA isozymes were inhibited by capsaicin in the micromolar range. This naturally bioactive compound has a Ki of 696.15 mu M against hCA I, and of 208.37 mu M against hCA II.