Inhibition Profiles of Some Symmetric Sulfamides Derived from Phenethylamines on Human Carbonic Anhydrase I, and II Isoenzymes. Issue 10 (16th September 2021)

• Record Type: Journal Article
• Authors: Topal, Fevzi; Aksu, Kadir; Gulcin, Ilhami; Tümer, Ferhan; Goksu, Süleyman
• Is Part Of: Chemistry & biodiversity. Volume 18:Issue 10(2021)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2021-09-16
• Subjects: ADME-Tox -- Carbonic anhydrase -- enzyme inhibition -- phenethylamine -- sulfamide; Biochemistry -- Periodicals; Molecular biology -- Periodicals; Biodiversity -- Periodicals; 572
• DOI: 10.1002/cbdv.202100422
• Languages: English
• ISSNs: 1612-1872

Abstract

Abstract: In this work, the inhibitory effect of some symmetric sulfamides derived from phenethylamines were determined against human carbonic anhydrase ( h CA) I, and II isoenzymes, and compared with standard compound acetazolamide. IC 50 values were obtained from the Enzyme activity (%)‐[Symmetric sulfamides] graphs. Also, K i values were calculated from the Lineweaver‐Burk graphs. Some symmetric sulfamides compounds (11 –18 ) demonstrated excellent inhibition effects against h CA I, and II isoenzymes. These compounds demonstrated effective inhibitory profiles with IC 50 values in ranging from 21.66–28.88 nM against h CA I, 14.44–30.13 nM against h CA II. Among these compounds, the best Ki value for h CA I ( K i : 8.34±1.60 nM) and h CA II ( K i : 16.40±1.00 nM) is compound number 11 . Besides, the IC 50 value of acetazolamide used as a standard was determined as h CA I, h CA II 57.75 nM, 49.50 nM, respectively. Moreover, in silico ADME‐Tox study showed that all synthesized compounds (11 –18 ) had good oral bioavailability in light of Jorgensen's rule of three, and of Lipinski's rule of five. Abstract :