Published January 1, 2016
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Kinetic and docking studies of cytosolic/tumor-associated carbonic anhydrase isozymes I, II and IX with some hydroxylic compounds
Creators
- 1. Bahcesehir Univ, Sch Med, Dept Biophys, Istanbul, Turkey
- 2. Ege Univ, Fac Sci, Dept Chem, Izmir, Turkey
- 3. Balikesir Univ, Sci & Art Fac, Dept Chem, Balikesir, Turkey
- 4. Univ Firenze, Lab Chim Bioinorgan, Polo Sci, Florence, Italy
- 5. Ondokuz Mayis Univ, Dept Agr Biotechnol, Fac Agr, Samsun, Turkey
- 6. Ibrahim Cecen Univ Agri, Art & Sci Fac, Dept Chem, Agri, Turkey
Description
A series of hydroxylic compounds (1-10, NK-154 and NK-168) have been assayed for the inhibition of three physiologically relevant carbonic anhydrase isozymes, the cytosolic isozymes I, II and tumor-associated isozyme IX. The investigated compounds showed inhibition constants in the range of 0.068-4003, 0.012-9.9 and 0.025-115 mm at the hCA I, hCA II and hCA IX enzymes, respectively. In order to investigate the binding mechanisms of these inhibitors, in silico studies were also applied. Molecular docking scores of the studied compounds are calculated using scoring algorithms, namely Glide/induced fit docking. The inhibitory potencies of the novel compounds were analyzed at the human isoforms hCA I, hCA II and hCA IX as targets and the K-I values were calculated.
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