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>

scholarly journals Synthesis and Human Carbonic Anhydrase I, II, IX, and XII Inhibition Studies of Sulphonamides Incorporating Mono-, Bi- and Tricyclic Imide Moieties

2021 ◽  
Vol 14 (7) ◽  
pp. 693
Author(s):  
Kalyan K. Sethi ◽  
KM Abha Mishra ◽  
Saurabh M. Verma ◽  
Daniela Vullo ◽  
Fabrizio Carta ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Carbonic Anhydrase ◽  
Docking Studies ◽  
Carbonic Anhydrases ◽  
Molecular Docking Studies ◽  
Structure Activity Relationships ◽  
Structure Activity ◽  
Carbonic Anhydrase I ◽  
Human Carbonic Anhydrase ◽  
Inhibition Studies

New derivatives were synthesised by reaction of amino-containing aromatic sulphonamides with mono-, bi-, and tricyclic anhydrides. These sulphonamides were investigated as human carbonic anhydrases (hCAs, EC 4.2.1.1) I, II, IX, and XII inhibitors. hCA I was inhibited with inhibition constants (Kis) ranging from 49 to >10,000 nM. The physiologically dominant hCA II was significantly inhibited by most of the sulphonamide with the Kis ranging between 2.4 and 4515 nM. hCA IX and hCA XII were inhibited by these sulphonamides in the range of 9.7 to 7766 nM and 14 to 316 nM, respectively. The structure–activity relationships (SAR) are rationalised with the help of molecular docking studies.

Crystal analysis of aromatic sulfonamide binding to native and (Zn)2 adduct of human carbonic anhydrase I Michigan 1

2002 ◽  
Vol 339 ◽  
pp. 135-144 ◽  
Author(s):  
Marta Ferraroni ◽  
Fabrizio Briganti ◽  
W.Richard Chegwidden ◽  
Claudiu T. Supuran ◽  
Andrea Scozzafava
Keyword(s):  
Carbonic Anhydrase ◽  
Carbonic Anhydrase I ◽  
Human Carbonic Anhydrase ◽  
Aromatic Sulfonamide

A simple enzyme-linked immunoassay of human carbonic anhydrase I for the study of developing erythroid cells

1990 ◽  
Vol 191 (3) ◽  
pp. 169-174 ◽  
Author(s):  
Takahito Kondo ◽  
Kazuhiro Murakami ◽  
Hiroshi Isobe ◽  
Naoyuki Taniguchi ◽  
Yoshikazu Kawakami
Keyword(s):  
Carbonic Anhydrase ◽  
Erythroid Cells ◽  
Carbonic Anhydrase I ◽  
Human Carbonic Anhydrase

scholarly journals New Histamine-Related Five-Membered N-Heterocycle Derivatives as Carbonic Anhydrase I Activators

Molecules ◽  
2022 ◽  
Vol 27 (2) ◽  
pp. 545
Author(s):  
Niccolò Chiaramonte ◽  
Alessio Gabellini ◽  
Andrea Angeli ◽  
Gianluca Bartolucci ◽  
Laura Braconi ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Imidazole Ring ◽  
Aliphatic Chain ◽  
Amino Group ◽  
Carbonic Anhydrase I ◽  
Terminal Amino ◽  
Human Carbonic Anhydrase ◽  
New Compounds ◽  
Related Compounds ◽  
Micromolar Range

A series of histamine (HST)-related compounds were synthesized and tested for their activating properties on five physiologically relevant human Carbonic Anhydrase (hCA) isoforms (I, II, Va, VII and XIII). The imidazole ring of HST was replaced with different 5-membered heterocycles and the length of the aliphatic chain was varied. For the most interesting compounds some modifications on the terminal amino group were also performed. The most sensitive isoform to activation was hCA I (KA values in the low micromolar range), but surprisingly none of the new compounds displayed activity on hCA II. Some derivatives (1, 3a and 22) displayed an interesting selectivity for activating hCA I over hCA II, Va, VII and XIII.

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.

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