Acyl selenoureido benzensulfonamides show potent inhibitory activity against carbonic anhydrases from the pathogenic bacterium Vibrio cholerae

Carbonic anhydrases (CAs, EC 4.2.1.1) catalyze the fundamental reaction of CO2 hydration in all living organisms and are actively involved in the regulation of a plethora of pathological and physiological conditions. A set of new coumarin/ dihydrocoumarin derivatives was here synthesized, characterized, and tested as human CA inhibitors. Their inhibitory activity was evaluated against the cytosolic human isoforms hCA I and II and the transmembrane hCA IX and hCA XII. Two compounds showed potent inhibitory activity against hCA IX, being more active or equipotent with the reference drug acetazolamide. Computational procedures were used to investigate the binding mode of this class of compounds within the active site of hCA IX and XII that are validated as anti-tumor targets.

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Activation studies of the α- and β-carbonic anhydrases from the pathogenic bacterium Vibrio cholerae with amines and amino acids

Journal of Enzyme Inhibition and Medicinal Chemistry ◽

10.1080/14756366.2017.1412316 ◽

2017 ◽

Vol 33 (1) ◽

pp. 227-233 ◽

Cited By ~ 5

Author(s):

Andrea Angeli ◽

Sonia Del Prete ◽

Sameh M. Osman ◽

Fatmah A. S. Alasmary ◽

Zeid AlOthman ◽

...

Keyword(s):

Amino Acids ◽

Vibrio Cholerae ◽

Pathogenic Bacterium ◽

Carbonic Anhydrases

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Comparison of the sulfonamide inhibition profiles of the α-, β- and γ-carbonic anhydrases from the pathogenic bacterium Vibrio cholerae

Bioorganic & Medicinal Chemistry Letters ◽

10.1016/j.bmcl.2016.03.014 ◽

2016 ◽

Vol 26 (8) ◽

pp. 1941-1946 ◽

Cited By ~ 30

Author(s):

Sonia Del Prete ◽

Daniela Vullo ◽

Viviana De Luca ◽

Vincenzo Carginale ◽

Sameh M. Osman ◽

...

Keyword(s):

Vibrio Cholerae ◽

Pathogenic Bacterium ◽

Carbonic Anhydrases

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Anion inhibition profiles of α-, β- and γ-carbonic anhydrases from the pathogenic bacterium Vibrio cholerae

Bioorganic & Medicinal Chemistry ◽

10.1016/j.bmc.2016.05.029 ◽

2016 ◽

Vol 24 (16) ◽

pp. 3413-3417 ◽

Cited By ~ 39

Author(s):

Sonia Del Prete ◽

Daniela Vullo ◽

Viviana De Luca ◽

Vincenzo Carginale ◽

Pietro di Fonzo ◽

...

Keyword(s):

Vibrio Cholerae ◽

Pathogenic Bacterium ◽

Carbonic Anhydrases

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Inhibition of α-, β- and γ-carbonic anhydrases from the pathogenic bacterium Vibrio cholerae with aromatic sulphonamides and clinically licenced drugs – a joint docking/molecular dynamics study

Journal of Enzyme Inhibition and Medicinal Chemistry ◽

10.1080/14756366.2020.1862102 ◽

2021 ◽

Vol 36 (1) ◽

pp. 469-479

Author(s):

Alessandro Bonardi ◽

Alessio Nocentini ◽

Sameh Mohamed Osman ◽

Fatmah Ali Alasmary ◽

Tahani Mazyad Almutairi ◽

...

Keyword(s):

Molecular Dynamics ◽

Vibrio Cholerae ◽

Pathogenic Bacterium ◽

Carbonic Anhydrases

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

International Journal of Molecular Sciences ◽

10.3390/ijms21093131 ◽

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.

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