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Bioorg Med Chem. 2015 May 15;23(10):2598-605. doi: 10.1016/j.bmc.2014.12.054. Epub 2015 Mar 20.

N-Acylsulfonamides strongly inhibit human carbonic anhydrase isoenzymes I and II.

Author information

1
Faculty of Science, Department of Chemistry, Atatürk University, 25240 Erzurum, Turkey.
2
Gumushane University, Vocational School of Health Services, Department of Medical Services and Techniques, Gumushane, Turkey.
3
Faculty of Science, Department of Chemistry, Atatürk University, 25240 Erzurum, Turkey. Electronic address: mcelik@atauni.edu.tr.
4
Faculty of Science, Department of Chemistry, Atatürk University, 25240 Erzurum, Turkey; Department of Zoology, College of Science, King Saud University, Riyadh, Saudi Arabia.
5
Università degli Studi di Firenze, Neurofarba Department, Rm. 66, via U. Schiff 6, I-50019 Sesto Fiorentino (Firenze), Italy.

Abstract

Sulfonamides represent a significant class of biologically active compounds that inhibit carbonic anhydrase (CA, EC.: 4.2.1.1) isoenzymes involved in different pathological and physiological events. Sulfonamide CA inhibitors are used therapeutically as diuretic, antiglaucoma, antiobesity and anticancer agents. A series of new sulfonamides were synthesized using imides and tosyl chloride as starting materials. These N-acylsulfonamides efficiently inhibited the cytosolic human carbonic anhydrase isoenzymes I, and II (hCA I, and II), with nanomolar range inhibition constants ranging between 36.4 ± 6.0-254.6 ± 18.0 and 58.3 ± 0.6-273.3 ± 2.5 nM, respectively.

KEYWORDS:

Carbonic anhydrase; Enzyme inhibition; Enzyme purification; Imide; N-Acylsulfonamide; Sulfonamide

PMID:
25863492
DOI:
10.1016/j.bmc.2014.12.054
[Indexed for MEDLINE]

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