Selective Inhibition of Human α-Thrombin by Cobalt(III) Schiff Base Complexes

Crystal structure of 2-[1-(2-chlorophenyl)-methylidene]hydrazino-1-(3,4- dihydroxyphenyl)ethanone monohydrate, C14H11ClN2O3 · H2O

“…These compounds play an important role in the development of coordination chemistry [1][2][3]. Some of the complexes derived from Schiff bases have been found to have pharmacological potential and antitumor activity [4][5][6]. Recently, we have reported a few Schiff base compounds [7][8][9].…”

Cobalt (III) Complexes as Novel Matrix Metalloproteinase-9 Inhibitors

“…[8][9][10][11] The cobalt(III) complexes bind histidine residues in active sites and on enzyme surfaces in a random fashion. Spectroscopic and chromatographic data suggested that the complexes bind to a histidine residue by axial ligand substitution.…”

“…Spectroscopic and chromatographic data suggested that the complexes bind to a histidine residue by axial ligand substitution. When an appropriate targeting group is attached, the cobalt(III) complexes can selectively inhibit the histidinecontaining enzymes such as thermolysin, 8 human α-thrombin, 9 and carbonic anhydrase. 9 Since histidine is the most commonly found residue in the active sites of zinc enzymes and zinc-binding proteins, 12 it has been demonstrated that the cobalt(III) complexes can interact with zinc finger proteins, such as HIV-1 nucleocapsid protein NCp7 and human zinc finger transcription factor Sp1.…”

Synthesis, Complexation and Biological Activity of New Isatin Schiff_bases

“…Isatin bis-Schiff bases are characterized by their capacity to co-ordinate to metal ions forming chelate rings 15 , act as inhibitors of human α-thrombin 16 and its copper(II) complex catalyzed the oxidation of carbohydrates 17 . Recently it has been reported that isatin bis-imine has antimicrobial properties 18 and affects cell viability 19 .…”