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Molecules 2014, 19(7), 10103-10114; doi:10.3390/molecules190710103

Capsaicin: A Potent Inhibitor of Carbonic Anhydrase Isoenzymes

Atatürk University, Faculty of Sciences, Department of Chemistry, Erzurum 25240, Turkey
Zoology Department, College of Science, King Saud University, Riyadh 11451, Saudi Arabia
Author to whom correspondence should be addressed.
Received: 6 May 2014 / Revised: 19 June 2014 / Accepted: 3 July 2014 / Published: 10 July 2014
(This article belongs to the Section Natural Products)
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Carbonic anhydrase (CA, EC 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
Keywords: capsaicin; carbonic anhydrase; enzyme purification; enzyme inhibition; affinity chromatography capsaicin; carbonic anhydrase; enzyme purification; enzyme inhibition; affinity chromatography

This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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MDPI and ACS Style

Arabaci, B.; Gulcin, I.; Alwasel, S. Capsaicin: A Potent Inhibitor of Carbonic Anhydrase Isoenzymes. Molecules 2014, 19, 10103-10114.

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