scholarly journals Inhibitory effects of benzimidazole containing new phenolic Mannich bases on human carbonic anhydrase isoforms hCA I and II

2016 ◽  
Vol 31 (6) ◽  
pp. 1540-1544 ◽  
Author(s):  
Halise Inci Gul ◽  
Zehra Yazici ◽  
Muhammet Tanc ◽  
Claudiu T. Supuran
Keyword(s):  
Carbonic Anhydrase ◽  
Mannich Bases ◽  
Inhibitory Effects ◽  
Human Carbonic Anhydrase

scholarly journals A Novel Ag-N-Heterocyclic Carbene Complex Bearing the Hydroxyethyl Ligand: Synthesis, Characterization, Crystal and Spectral Structures and Bioactivity Properties

Crystals ◽  
2020 ◽  
Vol 10 (3) ◽  
pp. 171 ◽  
Author(s):  
Aydin Aktas ◽  
Duygu Barut Celepci ◽  
Yetkin Gok ◽  
Parham Taslimi ◽  
Hulya Akincioglu ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Diffraction Method ◽  
Metabolic Enzymes ◽  
The Novel ◽  
X Ray Diffraction ◽  
Inhibitory Effects ◽  
Benzimidazolium Salt ◽  
Drug Potency ◽  
Human Carbonic Anhydrase

In this study, a novel silver N-heterocyclic carbene (Ag-NHC) complex bearing hydroxyethyl substituent has been synthesized from the hydroxyethyl-substituted benzimidazolium salt and silver oxide by using in-situ deprotonation method. A structure of the Ag-NHC complex was characterized by using UV-Vis, FTIR, 1H-NMR and 13C-NMR spectroscopies and elemental analysis techniques. Also, the crystal structure of the novel complex was determined by single-crystal X-ray diffraction method. In this paper, compound 1 showed excellent inhibitory effects against some metabolic enzymes. This complex had Ki of 1.14 0.26 µM against human carbonic anhydrase I (hCA I), 1.88±0.20 µM against human carbonic anhydrase II (hCA I), and 10.75±2.47 µM against α-glycosidase, respectively. On the other hand, the Ki value was found as 25.32±3.76 µM against acetylcholinesterase (AChE) and 41.31±7.42 µM against butyrylcholinesterase (BChE), respectively. These results showed that the complex had drug potency against some diseases related to using metabolic enzymes.

scholarly journals Synthesis and characterization of phenolic Mannich bases and effects of these compounds on human carbonic anhydrase isozymes I and II

2012 ◽  
Vol 28 (2) ◽  
pp. 337-342 ◽  
Author(s):  
Nurgün Büyükkıdan ◽  
Bülent Büyükkıdan ◽  
Metin Bülbül ◽  
Salih Özer ◽  
Hatice Gonca Yalçın
Keyword(s):  
Carbonic Anhydrase ◽  
Mannich Bases ◽  
Synthesis And Characterization ◽  
Human Carbonic Anhydrase

scholarly journals Microwave assisted solvent-free mannich bases: synthesis, characterization and effects of these compounds on HCA I and HCA II isozymes

2021 ◽  
Vol 40 (1) ◽  
pp. 43
Author(s):  
Bülent Büyükkıdan ◽  
Nurgün Büyükkıdan ◽  
Metin Bülbül ◽  
Melek Yılmaz ◽  
Evren Derrun Arslanbay ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Esterase Activity ◽  
Inhibitory Concentration ◽  
Mannich Bases ◽  
Solvent Free ◽  
Inhibitory Effects ◽  
Solvent Free Conditions ◽  
Control Compound ◽  
Esterase Activities

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.

Investigation of the Inhibitory Effects of Human Carbonic Anhydrase I and Jack Bean Urease by Coumarin Derivates

2018 ◽  
Vol 14 (3) ◽  
pp. 226-232
Author(s):  
Imdat Aygul ◽  
Fatma Yaylaci Karahalil ◽  
Ozkan Danis ◽  
Ayşe Ogan ◽  
Sevgi Kolayli
Keyword(s):  
Carbonic Anhydrase ◽  
Jack Bean Urease ◽  
Inhibitory Effects ◽  
Jack Bean ◽  
Carbonic Anhydrase I ◽  
Human Carbonic Anhydrase

Synthesis of N-alkyl (aril)-tetra pyrimidine thiones and investigation of their human carbonic anhydrase I and II inhibitory effects

2015 ◽  
Vol 31 (6) ◽  
pp. 1192-1197 ◽  
Author(s):  
Afsun Sujayev ◽  
Leyla Polat Kose ◽  
Emin Garibov ◽  
İlhami Gülçin ◽  
Vagif Farzaliev ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Inhibitory Effects ◽  
Carbonic Anhydrase I ◽  
Human Carbonic Anhydrase

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>

The inhibitory effects of phenolic Mannich bases on carbonic anhydrase I and II isoenzymes

2016 ◽  
Vol 31 (6) ◽  
pp. 1678-1681 ◽  
Author(s):  
Cem Yamali ◽  
Mehtap Tugrak ◽  
Halise Inci Gul ◽  
Muhammet Tanc ◽  
Claudiu T. Supuran
Keyword(s):  
Carbonic Anhydrase ◽  
Mannich Bases ◽  
Inhibitory Effects ◽  
Carbonic Anhydrase I

Dominant behaviours in the expression of human carbonic anhydrase hCA I activity

2014 ◽  
Vol 50 (59) ◽  
pp. 8043-8046 ◽  
Author(s):  
M. Yahia M. Abdelrahim ◽  
Muhammet Tanc ◽  
Jean-Yves Winum ◽  
Claudiu T. Supuran ◽  
Mihail Barboiu
Keyword(s):  
Carbonic Anhydrase ◽  
Inhibitory Effects ◽  
Human Carbonic Anhydrase

Dynamic deconvolution ofDCLsof inhibitors (CAIs) and activators (CAAs) of hCA I show that the inhibitory effects dominate over the activating ones.

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