Journal
MEDICINAL CHEMISTRY RESEARCH
Volume 26, Issue 8, Pages 1619-1627Publisher
SPRINGER BIRKHAUSER
DOI: 10.1007/s00044-017-1865-2
Keywords
Aryl pyrrolidine; Carbonic anhydrase; Isoenzymes; Enzyme inhibition; Enzyme purification
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Carbonic anhydrase isoenzymes are important metalloenzymes that are involved in many physiologic processes, in which they catalyze the reversible hydration of carbon dioxide (CO2) to bicarbonate (HCO3 (-)) and protons (H+) via a metal hydroxide nucleophilic mechanism. Because of their known biological activities and potential as carbonic anhydrase inhibitors, the present study focused on developing of a convenient route to synthesize 3-chloro-1-aryl pyrrolidine-2,5-diones (2b). This synthetic route started with (Z)-4-oxo-4-(arylamino)but-2-enoic acid (3b) and sulfurous dichloride (SOCl2) and resulted in a ring closing reaction that produced a series of 3-chloro-N-aryl maleimide derivatives (20-29) in good yields. This is the first report of the syntheses of 3-chloro-1-aryl pyyrolidine-2,5-diones 20-23 and 27-29 by ring-closing reactions of (Z)-4-oxo-4-(arylamino)but-2-enoic acid. The structures of all of the products were determined by H-1-NMR, C-13-NMR and infrared spectroscopy. Their biological activities were studied against human carbonic anhydrase I, and II. The 3-chloro-1-aryl pyrrolidine-2,5-diones strongly inhibited the activity of human carbonic anhydrase I and II, with K (i) values in the low nanomolar range of 23.27-36.83 nmol/L against human carbonic anhydrase I and 10.64-31.86 nmol/L against human carbonic anhydrase II.
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