Benazepril and Moexipril Inhibit the Esterase Activity of Carbonic Anhydrase I and II at Micromolar Concentration, an in Vitro Investigation

Mannich bases (2a–d) of aromatic amines were synthesized by using a conventional microwave technique under solvent-free conditions and characterized by IR and NMR (1H and 13C) and elemental analysis. The inhibitory effects of the synthesized Mannich bases were examined in vitro by using hydratase and esterase assays on carbonic anhydrase I and II isozymes (hCA, EC 4.2.1.1) purified from human erythrocyte cells. Acetazolamide was used as the control compound. The values of IC50, the half-maximum inhibitory concentration, were found for hydratase and esterase activities. Only two compounds (2b and 2d) exhibited poor hCA I and hCA II inhibition effects on esterase activity. In contrast, compounds 2a and 2c could be used as carbonic anhydrase activators as a result of the increased esterase activity of hCA I and hCA II isozymes.

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Synthesis and In Vitro Inhibition Effect of New Pyrido[2,3-d]pyrimidine Derivatives on Erythrocyte Carbonic Anhydrase I and II

BioMed Research International ◽

10.1155/2014/594879 ◽

2014 ◽

Vol 2014 ◽

pp. 1-8 ◽

Cited By ~ 7

Author(s):

Hilal Kuday ◽

Fatih Sonmez ◽

Cigdem Bilen ◽

Emre Yavuz ◽

Nahit Gençer ◽

...

Keyword(s):

Carbonic Anhydrase ◽

Inhibitory Activity ◽

Pyrimidine Derivatives ◽

Structure Activity ◽

Carbonic Anhydrase I ◽

Activity Structure ◽

In Vitro Inhibition ◽

Inhibitory Activities ◽

Erythrocyte Carbonic Anhydrase

In vitro inhibition effects of indolylchalcones and new pyrido[2,3-d]pyrimidine derivatives on purified human carbonic anhydrase I and II (hCA I and II) were investigated by using CO2as a substrate. The results showed that all compounds inhibited the hCA I and hCA II enzyme activities. Among all the synthesized compounds,7e(IC50=6.79 µM) was found to be the most active compound for hCA I inhibitory activity and5g(IC50=7.22 µM) showed the highest hCA II inhibitory activity. Structure-activity relationships study showed that indolylchalcone derivatives have higher inhibitory activities than pyrido[2,3-d]pyrimidine derivatives on hCA I and hCA II. Additionally, methyl group bonded to uracil ring increases inhibitory activities on both hCA I and hCA II.

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In vitro inhibition of purified human carbonic anhydrase I and II by novel fluorene derivatives

Macedonian Journal of Chemistry and Chemical Engineering ◽

10.20450/mjcce.2014.440 ◽

2014 ◽

Vol 33 (2) ◽

pp. 199 ◽

Cited By ~ 2

Author(s):

Hülya Demirhan ◽

Mustafa Arslan ◽

Mustafa Oguzhan Kaya ◽

Yeşim Kaya ◽

Nahit Gençer ◽

...

Keyword(s):

Carbonic Anhydrase ◽

Human Erythrocytes ◽

Affinity Column ◽

Inhibitory Effects ◽

Thiourea Derivatives ◽

Carbonic Anhydrase I ◽

In Vitro Inhibition ◽

Human Carbonic Anhydrase ◽

Sepharose 4B

In this study, 9-benzylidene-9H-fluorene-substituted urea (5a–p) and thiourea derivatives (5q–v) were synthesized and their inhibitory effects on the activity of human carbonic anhydrase (hCA) I and II were evaluated. hCA I and II were purified from human erythrocytes using a Sepharose 4B-L-tyrosine-sulphanilamide affinity column. All the synthesized compounds inhibited the activity of the hCA I and II isoenzymes. Among the synthesized compounds, 5f was found to be the most active (IC50 = 21.4 μM) for inhibition of hCA I and 5s was the most active (IC50 = 25.3 μM) for inhibition of hCA II.

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