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Design of [(2-pyrimidinylthio)acetyl]benzenesulfonamides as inhibitors of human carbonic anhydrases.

Čapkauskaitė E, Zubrienė A, Baranauskienė L, Tamulaitienė G, Manakova E, Kairys V, Gražulis S, Tumkevičius S, Matulis D
Eur J Med Chem 51 259-70 (2012)
Related entries: 3m2n, 3s8x, 3s9t, 3sap, 3sax, 3sbh

Cited: 18 times
EuropePMC logo PMID: 22440859

Abstract

A series of [(2-pyrimidinylthio)acetyl]benzenesulfonamides were designed and synthesized. Their binding affinities as inhibitors of several recombinant human carbonic anhydrase (CA) isozymes were determined by isothermal titration calorimetry (ITC) and thermal shift assay (TSA). A group of compounds containing a chlorine atom in the benzenesulfonamide ring were found to exhibit higher selectivity but lower binding affinity toward tested CAs. The crystal structures of selected compounds in complex with CA II were determined to atomic resolution. Docking studies were performed to compare the binding modes of experimentally determined crystallographic structures with computational prediction of the pyrimidine derivative binding to CA II. Several compounds bound to select CAs with single-digit nanomolar affinities and could be used as leads for inhibitor development toward a select CA isozyme.

Articles - 3sbi mentioned but not cited (1)

  1. Crystal structure correlations with the intrinsic thermodynamics of human carbonic anhydrase inhibitor binding. Smirnov A, Zubrienė A, Manakova E, Gražulis S, Matulis D. PeerJ 6 e4412 (2018)


Reviews citing this publication (3)

  1. Reconsidering anion inhibitors in the general context of drug design studies of modulators of activity of the classical enzyme carbonic anhydrase. Nocentini A, Angeli A, Carta F, Winum JY, Zalubovskis R, Carradori S, Capasso C, Donald WA, Supuran CT. J Enzyme Inhib Med Chem 36 561-580 (2021)
  2. Focus on molecular events in the anterior chamber leading to glaucoma. Saccà SC, Izzotti A. Cell Mol Life Sci 71 2197-2218 (2014)
  3. Thermodynamic, kinetic, and structural parameterization of human carbonic anhydrase interactions toward enhanced inhibitor design. Linkuvienė V, Zubrienė A, Manakova E, Petrauskas V, Baranauskienė L, Zakšauskas A, Smirnov A, Gražulis S, Ladbury JE, Matulis D. Q Rev Biophys 51 e10 (2018)

Articles citing this publication (14)

  1. Combining the tail and the ring approaches for obtaining potent and isoform-selective carbonic anhydrase inhibitors: solution and X-ray crystallographic studies. Bozdag M, Ferraroni M, Nuti E, Vullo D, Rossello A, Carta F, Scozzafava A, Supuran CT. Bioorg Med Chem 22 334-340 (2014)
  2. Structure-based screening for the discovery of new carbonic anhydrase VII inhibitors. De Luca L, Ferro S, Damiano FM, Supuran CT, Vullo D, Chimirri A, Gitto R. Eur J Med Chem 71 105-111 (2014)
  3. Benzenesulfonamides with pyrimidine moiety as inhibitors of human carbonic anhydrases I, II, VI, VII, XII, and XIII. Čapkauskaitė E, Zubrienė A, Smirnov A, Torresan J, Kišonaitė M, Kazokaitė J, Gylytė J, Michailovienė V, Jogaitė V, Manakova E, Gražulis S, Tumkevičius S, Matulis D. Bioorg Med Chem 21 6937-6947 (2013)
  4. Picomolar inhibitors of carbonic anhydrase: Importance of inhibition and binding assays. Smirnovienė J, Smirnovas V, Matulis D. Anal Biochem 522 61-72 (2017)
  5. Benzenesulfonamides with benzimidazole moieties as inhibitors of carbonic anhydrases I, II, VII, XII and XIII. Zubrienė A, Čapkauskaitė E, Gylytė J, Kišonaitė M, Tumkevičius S, Matulis D. J Enzyme Inhib Med Chem 29 124-131 (2014)
  6. 4-amino-substituted benzenesulfonamides as inhibitors of human carbonic anhydrases. Rutkauskas K, Zubrienė A, Tumosienė I, Kantminienė K, Kažemėkaitė M, Smirnov A, Kazokaitė J, Morkūnaitė V, Čapkauskaitė E, Manakova E, Gražulis S, Beresnevičius ZJ, Matulis D. Molecules 19 17356-17380 (2014)
  7. Intrinsic Thermodynamics and Structure Correlation of Benzenesulfonamides with a Pyrimidine Moiety Binding to Carbonic Anhydrases I, II, VII, XII, and XIII. Kišonaitė M, Zubrienė A, Capkauskaitė E, Smirnov A, Smirnovienė J, Kairys V, Michailovienė V, Manakova E, Gražulis S, Matulis D. PLoS One 9 e114106 (2014)
  8. Monoclonal antibodies raised against 167-180 aa sequence of human carbonic anhydrase XII inhibit its enzymatic activity. Dekaminaviciute D, Kairys V, Zilnyte M, Petrikaite V, Jogaite V, Matuliene J, Gudleviciene Z, Vullo D, Supuran CT, Zvirbliene A. J Enzyme Inhib Med Chem 29 804-810 (2014)
  9. Saccharin sulfonamides as inhibitors of carbonic anhydrases I, II, VII, XII, and XIII. Morkūnaitė V, Baranauskienė L, Zubrienė A, Kairys V, Ivanova J, Trapencieris P, Matulis D. Biomed Res Int 2014 638902 (2014)
  10. Carbohydrazones as new class of carbonic anhydrase inhibitors: Synthesis, kinetics, and ligand docking studies. Iqbal S, Saleem M, Azim MK, Taha M, Salar U, Khan KM, Perveen S, Choudhary MI. Bioorg Chem 72 89-101 (2017)
  11. Methyl 2-Halo-4-Substituted-5-Sulfamoyl-Benzoates as High Affinity and Selective Inhibitors of Carbonic Anhydrase IX. Zakšauskas A, Čapkauskaitė E, Paketurytė-Latvė V, Smirnov A, Leitans J, Kazaks A, Dvinskis E, Stančaitis L, Mickevičiūtė A, Jachno J, Jezepčikas L, Linkuvienė V, Sakalauskas A, Manakova E, Gražulis S, Matulienė J, Tars K, Matulis D. Int J Mol Sci 23 130 (2021)
  12. Carbonic Anhydrase and Urease Inhibitory Potential of Various Plant Phenolics Using in vitro and in silico Methods. Rauf A, Raza M, Saleem M, Ozgen U, Karaoglan ES, Renda G, Palaska E, Orhan IE. Chem Biodivers 14 (2017)
  13. Switching the Inhibitor-Enzyme Recognition Profile via Chimeric Carbonic Anhydrase XII. Smirnovienė J, Smirnov A, Zakšauskas A, Zubrienė A, Petrauskas V, Mickevičiūtė A, Michailovienė V, Čapkauskaitė E, Manakova E, Gražulis S, Baranauskienė L, Chen WY, Ladbury JE, Matulis D. ChemistryOpen 10 567-580 (2021)
  14. Biochemical and in silico inhibition of bovine and human carbonic anhydrase-II by 1H-1,2,3-triazole analogs. Khan M, Avula SK, Halim SA, Waqas M, Asmari M, Khan A, Al-Harrasi A. Front Chem 10 1072337 (2022)


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