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Substituted benzene sulfonamides incorporating 1,3,5-triazinyl moieties potently inhibit human carbonic anhydrases II, IX and XII.
Bioorg Med Chem Lett. 2014 Mar 01; 24(5):1310-4.BM

Abstract

A series of benzene sulfonamides incorporating 1,3,5-triazinyl moieties were synthesized using cyanuric chloride as starting material. Inhibition studies against human carbonic anhydrase (hCA, EC 4.2.1.1) isoforms I, II (cytosolic) and IX, XII (transmembrane, tumor-associated) isoforms were performed with the new compounds. hCA I was modestly inhibited (KIs in the range of 87 nM-4.35 μM), hCA II was moderately inhibited by most of the new compounds (KIs in the range of 12.5-130 nM), whereas the tumor associated isoforms were potently inhibited, with KIs in the range of 1.2-34.1 nM against hCA IX and of 2.1-33.9 against hCA XII, respectively. Docking studies of some of the new compounds showed an effective binding mode within the enzyme active site, as demonstrated earlier by X-ray crystallography for structurally-related sulfonamides incorporating 1,3,5-triazinyl functionalities.

Authors+Show Affiliations

Shri G.S. Institute of Technology and Science, Department of Pharmacy, 23, Park Road, Indore 452003, Madhya Pradesh, India.Shri G.S. Institute of Technology and Science, Department of Pharmacy, 23, Park Road, Indore 452003, Madhya Pradesh, India. Electronic address: mtiwari@sgsits.ac.in.Università degli Studi di Firenze, Dipartimento di Chimica, Lab. Chimica Bioinorganica, Via della Lastruccia 3, 50019 Sesto Fiorentino (Florence), Italy; Università degli Studi di Firenze, NEUROFARBA Dept., Sezione di Scienze Farmaceutiche e Nutraceutiche, Via Ugo Schiff 6, I-50019 Sesto Fiorentino (Florence), Italy.Università degli Studi di Firenze, Dipartimento di Chimica, Lab. Chimica Bioinorganica, Via della Lastruccia 3, 50019 Sesto Fiorentino (Florence), Italy; Università degli Studi di Firenze, NEUROFARBA Dept., Sezione di Scienze Farmaceutiche e Nutraceutiche, Via Ugo Schiff 6, I-50019 Sesto Fiorentino (Florence), Italy. Electronic address: claudiu.supuran@unifi.it.

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

24507918

Citation

Saluja, Amrita K., et al. "Substituted Benzene Sulfonamides Incorporating 1,3,5-triazinyl Moieties Potently Inhibit Human Carbonic Anhydrases II, IX and XII." Bioorganic & Medicinal Chemistry Letters, vol. 24, no. 5, 2014, pp. 1310-4.
Saluja AK, Tiwari M, Vullo D, et al. Substituted benzene sulfonamides incorporating 1,3,5-triazinyl moieties potently inhibit human carbonic anhydrases II, IX and XII. Bioorg Med Chem Lett. 2014;24(5):1310-4.
Saluja, A. K., Tiwari, M., Vullo, D., & Supuran, C. T. (2014). Substituted benzene sulfonamides incorporating 1,3,5-triazinyl moieties potently inhibit human carbonic anhydrases II, IX and XII. Bioorganic & Medicinal Chemistry Letters, 24(5), 1310-4. https://doi.org/10.1016/j.bmcl.2014.01.048
Saluja AK, et al. Substituted Benzene Sulfonamides Incorporating 1,3,5-triazinyl Moieties Potently Inhibit Human Carbonic Anhydrases II, IX and XII. Bioorg Med Chem Lett. 2014 Mar 1;24(5):1310-4. PubMed PMID: 24507918.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Substituted benzene sulfonamides incorporating 1,3,5-triazinyl moieties potently inhibit human carbonic anhydrases II, IX and XII. AU - Saluja,Amrita K, AU - Tiwari,Meena, AU - Vullo,Daniela, AU - Supuran,Claudiu T, Y1 - 2014/01/27/ PY - 2013/12/10/received PY - 2014/01/18/revised PY - 2014/01/20/accepted PY - 2014/2/11/entrez PY - 2014/2/11/pubmed PY - 2014/10/29/medline KW - 1,3,5-Triazine KW - Benzene sulfonamides KW - Carbonic anhydrase KW - Enzyme inhibition KW - Isoform selectivity KW - Molecular docking SP - 1310 EP - 4 JF - Bioorganic & medicinal chemistry letters JO - Bioorg. Med. Chem. Lett. VL - 24 IS - 5 N2 - A series of benzene sulfonamides incorporating 1,3,5-triazinyl moieties were synthesized using cyanuric chloride as starting material. Inhibition studies against human carbonic anhydrase (hCA, EC 4.2.1.1) isoforms I, II (cytosolic) and IX, XII (transmembrane, tumor-associated) isoforms were performed with the new compounds. hCA I was modestly inhibited (KIs in the range of 87 nM-4.35 μM), hCA II was moderately inhibited by most of the new compounds (KIs in the range of 12.5-130 nM), whereas the tumor associated isoforms were potently inhibited, with KIs in the range of 1.2-34.1 nM against hCA IX and of 2.1-33.9 against hCA XII, respectively. Docking studies of some of the new compounds showed an effective binding mode within the enzyme active site, as demonstrated earlier by X-ray crystallography for structurally-related sulfonamides incorporating 1,3,5-triazinyl functionalities. SN - 1464-3405 UR - https://www.unboundmedicine.com/medline/citation/24507918/Substituted_benzene_sulfonamides_incorporating_135_triazinyl_moieties_potently_inhibit_human_carbonic_anhydrases_II_IX_and_XII_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0960-894X(14)00078-X DB - PRIME DP - Unbound Medicine ER -