Anion inhibition studies of the β-carbonic anhydrase from the pathogenic bacterium Vibrio cholerae

2016 ◽  
Vol 26 (5) ◽  
pp. 1406-1410 ◽  
Author(s):  
Daniela Vullo ◽  
Sonia Del Prete ◽  
Viviana De Luca ◽  
Vincenzo Carginale ◽  
Marta Ferraroni ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Vibrio Cholerae ◽  
Pathogenic Bacterium ◽  
Inhibition Studies

Anion inhibition studies of the α-carbonic anhydrase from the pathogenic bacterium Vibrio cholerae

2013 ◽  
Vol 23 (6) ◽  
pp. 1636-1638 ◽  
Author(s):  
Daniela Vullo ◽  
Semra Isik ◽  
Sonia Del Prete ◽  
Viviana De Luca ◽  
Vincenzo Carginale ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Vibrio Cholerae ◽  
Pathogenic Bacterium ◽  
Inhibition Studies

DNA Cloning, Characterization, and Inhibition Studies of an α-Carbonic Anhydrase from the Pathogenic Bacterium Vibrio cholerae

2012 ◽  
Vol 55 (23) ◽  
pp. 10742-10748 ◽  
Author(s):  
Sonia Del Prete ◽  
Semra Isik ◽  
Daniela Vullo ◽  
Viviana De Luca ◽  
Vincenzo Carginale ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Vibrio Cholerae ◽  
Pathogenic Bacterium ◽  
Dna Cloning ◽  
Inhibition Studies

Sulfonamide inhibition studies of the β-carbonic anhydrase from the pathogenic bacterium Vibrio cholerae

2016 ◽  
Vol 24 (5) ◽  
pp. 1115-1120 ◽  
Author(s):  
Sonia Del Prete ◽  
Daniela Vullo ◽  
Viviana De Luca ◽  
Vincenzo Carginale ◽  
Marta Ferraroni ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Vibrio Cholerae ◽  
Pathogenic Bacterium ◽  
Inhibition Studies

The γ-carbonic anhydrase from the pathogenic bacterium Vibrio cholerae is potently activated by amines and amino acids

2018 ◽  
Vol 77 ◽  
pp. 1-5 ◽  
Author(s):  
Andrea Angeli ◽  
Sonia Del Prete ◽  
William A. Donald ◽  
Clemente Capasso ◽  
Claudiu T. Supuran
Keyword(s):  
Amino Acids ◽  
Carbonic Anhydrase ◽  
Vibrio Cholerae ◽  
Pathogenic Bacterium

scholarly journals Biochemical properties of a new α-carbonic anhydrase from the human pathogenic bacterium, Vibrio cholerae

2013 ◽  
Vol 29 (1) ◽  
pp. 23-27 ◽  
Author(s):  
Sonia Del Prete ◽  
Viviana De Luca ◽  
Andrea Scozzafava ◽  
Vincenzo Carginale ◽  
Claudiu T. Supuran ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Vibrio Cholerae ◽  
Biochemical Properties ◽  
Pathogenic Bacterium ◽  
Human Pathogenic Bacterium

scholarly journals Novel Indole-Based Hydrazones as Potent Inhibitors of the α-class Carbonic Anhydrase from Pathogenic Bacterium Vibrio cholerae

2020 ◽  
Vol 21 (9) ◽  
pp. 3131
Author(s):  
Kübra Demir-Yazıcı ◽  
Özlen Güzel-Akdemir ◽  
Andrea Angeli ◽  
Claudiu T. Supuran ◽  
Atilla Akdemir
Keyword(s):  
Vibrio Cholerae ◽  
Active Site ◽  
Selective Inhibition ◽  
Pathogenic Bacterium ◽  
Carbonic Anhydrases ◽  
Urgent Problem ◽  
Antimicrobial Drugs ◽  
Molecular Modeling Studies ◽  
Inhibitory Activities ◽  
Inhibition Studies

Due to the increasing resistance of currently used antimicrobial drugs, there is an urgent problem for the treatment of cholera disease, selective inhibition of the α-class carbonic anhydrases (CA, EC 4.2.1.1) from the pathogenic bacterium Vibrio cholerae (VcCA) presents an alternative therapeutic target. In this study, a series of hydrazone derivatives, carrying the 2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide scaffold, have been evaluated as inhibitors of the VcCA with molecular modeling studies. The results suggest that these compounds may bind to the active site of VcCA. To verify this, VcCA enzyme inhibition studies were performed and as predicted most of the tested compounds displayed potent inhibitory activities against VcCA with three compounds showing KI values lower than 30 nM. In addition, all these compounds showed selectivity for VcCA and the off-targets hCA I and II.

Coumaronochromone as antibacterial and carbonic anhydrase inhibitors from Aerva persica (Burm.f.) Merr.: experimental and first-principles approaches

2020 ◽  
Vol 0 (0) ◽  
Author(s):  
Muhammad Imran ◽  
Ahmad Irfan ◽  
Mohammed A. Assiri ◽  
Sajjad H. Sumrra ◽  
Muhammad Saleem ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
First Principles ◽  
Molecular Electrostatic Potential ◽  
Chemical Constituents ◽  
Bacterial Strains ◽  
Hirshfeld Analysis ◽  
Carbonic Anhydrase Inhibition ◽  
Inhibition Studies ◽  
Lowest Unoccupied Molecular Orbitals

AbstractThe Aerva plants are exceptionally rich in phytochemicals and possess therapeutics potential. Phytochemical screening shows that Aerva persica (Burm.f.) Merr. contains highest contents i.e., total phenolics, flavonoids, flavonols, tannins, alkaloids, carbohydrates, anthraquinones and glycosides. In-vitro antibacterial and enzymatic (carbonic anhydrase) inhibition studies on methanol extracts of A. persica indicated the presence of biological active constituents within chloroform soluble portions. Investigation in the pure constituents on the chloroform portions of A. persica accomplished by column chromatography, NMR and MS analysis. The bioguided isolation yields four chemical constituents of coumaronochromone family, namely aervin (1-4). These pure chemical entities (1-4) showed significant antibacterial activity in the range of 60.05–79.21 µg/ml against various bacterial strains using ampicillin and ciprofloxacin as standard drugs. The compounds 1-4 showed promising carbonic anhydrase inhibition with IC50 values of 19.01, 18.24, 18.65 and 12.92 µM, respectively, using standard inhibitor acetazolamide. First-principles calculations revealed comprehensive intramolecular charge transfer in the studied compounds 1-4. The spatial distribution of highest occupied and lowest unoccupied molecular orbitals, ionization potential, molecular electrostatic potential and Hirshfeld analysis revealed that these coumaronochromone compounds would be proficient biological active compounds. These pure constituents may be used as a new pharmacophore to treat leaukomia, epilepsy, glaucoma and cystic fibrosis.

scholarly journals Anion inhibition studies of the Zn(II)-bound ι-carbonic anhydrase from the Gram-negative bacterium Burkholderia territorii

2021 ◽  
Vol 36 (1) ◽  
pp. 372-376
Author(s):  
Andrea Petreni ◽  
Viviana De Luca ◽  
Andrea Scaloni ◽  
Alessio Nocentini ◽  
Clemente Capasso ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Negative Bacterium ◽  
Gram Negative ◽  
Inhibition Studies

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.

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