Inhibition Profiles of Some Symmetric Sulfamides Derived from Phenethylamines on Human Carbonic Anhydrase I, and II Isoenzymes

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Atıf İçin Kopyala

Topal F., Aksu K., Gülçin İ., Tümer F., Göksu S.

CHEMISTRY & BIODIVERSITY, cilt.18, sa.10, 2021 (SCI-Expanded)

• Yayın Türü: Makale / Tam Makale
• Cilt numarası: 18 Sayı: 10
• Basım Tarihi: 2021
• Doi Numarası: 10.1002/cbdv.202100422
• Dergi Adı: CHEMISTRY & BIODIVERSITY
• Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Aquatic Science & Fisheries Abstracts (ASFA), CAB Abstracts, Chemical Abstracts Core, EMBASE, MEDLINE, Veterinary Science Database
• Anahtar Kelimeler: ADME-Tox, Carbonic anhydrase, enzyme inhibition, phenethylamine, sulfamide, ACETYLCHOLINE ESTERASE, HCA I, DERIVATIVES, VITRO, PHENYLETHYLAMINE, PURIFICATION, BUTYRYLCHOLINESTERASE, LACTOPEROXIDASE, SULFONAMIDES, DISCOVERY
• Atatürk Üniversitesi Adresli: Evet

Özet

In this work, the inhibitory effect of some symmetric sulfamides derived from phenethylamines were determined against human carbonic anhydrase (hCA) I, and II isoenzymes, and compared with standard compound acetazolamide. IC50 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 hCA I, and II isoenzymes. These compounds demonstrated effective inhibitory profiles with IC50 values in ranging from 21.66-28.88 nM against hCA I, 14.44-30.13 nM against hCA II. Among these compounds, the best K-i value for hCA I (K-i: 8.34 +/- 1.60 nM) and hCA II (K-i: 16.40 +/- 1.00 nM) is compound number 11. Besides, the IC50 value of acetazolamide used as a standard was determined as hCA I, hCA 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.