Kinetic and docking studies of cytosolic/tumor-associated carbonic anhydrase isozymes I, II and IX with some hydroxylic compounds.

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.

Synthesis, X-ray structural and thermal analysis of a novel copper compound containing dissymmetric independent 5- and 6-coordinate CuL(H2O)n (n = 2, 3) units and hydrogen bond bridges.

The synthesis, thermogravimetric and X-ray structure analysis of a highly unusual copper compound prepared from a chiral tridentate Schiff base ligand is reported. The title compound [CuL(H(2)O(2)]. CuL(H(2)O(3)].

Synthesis and biological activity of novel thiourea derivatives as carbonic anhydrase inhibitors.

A new series of chiral thiourea derivatives (5a-5c) and thiourea containing benzimidazole moieties (9b-9e) were synthesized from different amino acids (l-valine, l-isoleucine, l-methionine, l-phenylalanine, and d-phenylglycine). The compounds were characterized and tested against the two most studied members of the pH regulatory enzyme family, carbonic anhydrase (CA, EC 4.2.