Capsaicin: A Potent Inhibitor of Carbonic Anhydrase Isoenzymes
AbstractCarbonic anhydrase (CA, EC 220.127.116.11) 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 µM against hCA I, and of 208.37 µM against hCA II. View Full-Text
Scifeed alert for new publicationsNever miss any articles matching your research from any publisher
- Get alerts for new papers matching your research
- Find out the new papers from selected authors
- Updated daily for 49'000+ journals and 6000+ publishers
- Define your Scifeed now
Arabaci, B.; Gulcin, I.; Alwasel, S. Capsaicin: A Potent Inhibitor of Carbonic Anhydrase Isoenzymes. Molecules 2014, 19, 10103-10114.
Arabaci B, Gulcin I, Alwasel S. Capsaicin: A Potent Inhibitor of Carbonic Anhydrase Isoenzymes. Molecules. 2014; 19(7):10103-10114.Chicago/Turabian Style
Arabaci, Betul; Gulcin, Ilhami; Alwasel, Saleh. 2014. "Capsaicin: A Potent Inhibitor of Carbonic Anhydrase Isoenzymes." Molecules 19, no. 7: 10103-10114.