The behavior of some chalcones on acetylcholinesterase and carbonic anhydrase activity

• Published in: Drug and chemical toxicology (New York, N.Y. 1978) Vol. 42; no. 6; pp. 634 - 640
• Main Authors: Aslan, Hatice Esra, Demir, Yeliz, Özaslan, Muhammet Serhat, Türkan, Fikret, Beydemir, Şükrü, Küfrevioğlu, Ömer Irfan
• Format: Journal Article
• Language: English
• Published: United States Taylor & Francis 02.11.2019
• Subjects: Acetylcholinesterase; carbonic anhydrase; chalcone; inhibition; purification; chalcone; carbonic anhydrase; inhibition; Acetylcholinesterase; purification
• ISSN: 0148-0545; 1525-6014
• DOI: 10.1080/01480545.2018.1463242

Carbonic anhydrase (CA) has a key role in respiration, carbon dioxide and bicarbonate transport. Acetylcholinesterase (AChE) is a serine hydrolase and mostly abundant at neuromuscular junctions and cholinergic brain synapses. Inhibitors of these enzymes could aid in illuminating the role in disease processes. In this study, we separately purified CA I and CA II from human erythrocytes. The purity of the enzymes was showed by SDS-PAGE analysis. We also investigated the inhibition of seven chalcones toward hCA I, hCA II, and AChE. The chalcones were effective inhibitors of the cytosolic CA isoforms (hCA I and hCA II) and AChE with K i values in the range of 1.83-7.05 μM for hCA I, 0.59-5.50 μM for hCA II, and 0.61-86.11 μM for AChE. All compounds were showed competitive inhibition aganist both enzymes. These compounds can be a potent inhibitor of AChE enzyme and both cytosolic CA isoenzymes which are commonly used in the pharmaceutical and medical industries.