Carbonic anhydrase inhibitors: in vitro inhibition of α isoforms (hCA I, hCA II, bCA III, hCA IV) by flavonoids

2011 ◽  
Vol 28 (2) ◽  
pp. 283-288 ◽  
Author(s):  
Derya Ekinci ◽  
Lutfi Karagoz ◽  
Deniz Ekinci ◽  
Murat Senturk ◽  
Claudiu T. Supuran
Keyword(s):  
Carbonic Anhydrase ◽  
Carbonic Anhydrase Inhibitors ◽  
In Vitro Inhibition

scholarly journals Carbonic Anhydrase Inhibitors. Part 551 Metal Complexes of 1,3,4-Thiadiazole-2-Sulfonamide Derivatives: In Vitro Inhibition Studies With Carbonic Anhydrase Isozymes I, II and IV

1998 ◽  
Vol 5 (2) ◽  
pp. 103-114 ◽  
Author(s):  
Claudiu T. Supuran ◽  
Andrea Scozzafava ◽  
Fabrizio Briganti ◽  
Marc A. Ilies ◽  
Andrei Jitianu
Keyword(s):  
Carbonic Anhydrase ◽  
Metal Complexes ◽  
Coordination Compounds ◽  
Active Sites ◽  
Carbonic Anhydrase Inhibitors ◽  
Standard Procedures ◽  
In Vitro Inhibition ◽  
Characteristic Features ◽  
Inhibition Studies

Coordination compounds of 5-chloroacetamido-1,3,4-thiadiazole-2-sulfonamide (Hcaz) with V(IV), Cr(lll), Fe(ll), Co(ll), Ni(ll) and Cu(ll) have been prepared and characterized by standard procedures (spectroscopic, magnetic, EPR, thermogravimetric and conductimetric measurements). Some of these compounds showed very good in vitro inhibitory properties against three physiologically relevant carbonic anhydrase (CA)isozymes, i.e., CA I, II, and IV. The differences between these isozymes in susceptibility to inhibition by these metal complexes is discussed in relationship to the characteristic features of their active sites, and is rationalized in terms useful for developing isozyme-specific CA inhibitors.

New coumarin/sulfocoumarin linked phenylacrylamides as selective transmembrane carbonic anhydrase inhibitors: Synthesis and in-vitro biological evaluation

2020 ◽  
Vol 28 (15) ◽  
pp. 115586
Author(s):  
Baijayantimala Swain ◽  
Andrea Angeli ◽  
Priti Singh ◽  
Claudiu T. Supuran ◽  
Mohammed Arifuddin
Keyword(s):  
Carbonic Anhydrase ◽  
Biological Evaluation ◽  
Carbonic Anhydrase Inhibitors

Discovery of potent anti-convulsant carbonic anhydrase inhibitors: Design, synthesis, in vitro and in vivo appraisal

2018 ◽  
Vol 156 ◽  
pp. 430-443 ◽  
Author(s):  
Chandra Bhushan Mishra ◽  
Shikha Kumari ◽  
Andrea Angeli ◽  
Silvia Bua ◽  
Martina Buonanno ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Carbonic Anhydrase Inhibitors ◽  
Design Synthesis

In vitro inhibition of salicylic acid derivatives on human cytosolic carbonic anhydrase isozymes I and II

2008 ◽  
Vol 16 (20) ◽  
pp. 9101-9105 ◽  
Author(s):  
Esra Bayram ◽  
Murat Senturk ◽  
O. Irfan Kufrevioglu ◽  
Claudiu T. Supuran
Keyword(s):  
Salicylic Acid ◽  
Carbonic Anhydrase ◽  
Salicylic Acid Derivatives ◽  
In Vitro Inhibition

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

2014 ◽  
Vol 2014 ◽  
pp. 1-8 ◽  
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.

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

2014 ◽  
Vol 33 (2) ◽  
pp. 199 ◽  
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

<p>In this study, 9-benzylidene-9<em>H</em>-fluorene-substituted urea (<strong>5a–p</strong>) and thiourea derivatives <strong>(5q–v)</strong> 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, <strong>5f</strong><strong> </strong>was found to be the most active (IC<sub>50</sub> = 21.4 μM) for inhibition of hCA I and <strong>5s </strong>was the most active (IC<sub>50</sub> = 25.3 μM) for inhibition of<strong> </strong>hCA II.</p><p><strong><br /></strong></p>

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