Synthesis and characterization of a proton transfer salt between 2,6-pyridinedicarboxylic acid and 2-aminobenzothiazole, and its complexes and their inhibition studies on carbonic anhydrase isoenzymes


Creative Commons License

İLKİMEN H., YENİKAYA C., SARI M., BÜLBÜL M., TUNCA E., DAL H.

JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, vol.29, no.3, pp.353-361, 2014 (Peer-Reviewed Journal) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 29 Issue: 3
  • Publication Date: 2014
  • Doi Number: 10.3109/14756366.2013.782299
  • Journal Name: JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
  • Journal Indexes: Science Citation Index Expanded, Scopus
  • Page Numbers: pp.353-361
  • Keywords: 2-Aminobenzothiazole, carbonic anydrase, dipicolinic acid, inhibition, proton transfer, BIOLOGICAL EVALUATION, DERIVATIVES, BENZOTHIAZOLES, BENZOXAZOLE, COMPOUND, ESTERASE, BEHAVIOR, CRYSTAL, SPECTRA, POTENT

Abstract

A novel proton transfer compound (HABT)(+)(Hdipic)(-) (1) obtained from ABT and H(2)dipic and its metal complexes (2-5) have been prepared and characterized by spectroscopic techniques. Single crystal X-ray diffraction method has also been applied to 2 and 5. While complex 2 has a distorted octahedral conformation, 5 exhibits a distorted square pyramidal structure. The structures of 3 and 4 might be proposed as octahedral according to experimental data. All compounds were also evaluated for their in vitro inhibition effects on hCA I and II for their hydratase and esterase activities. Although there is no inhibition for hydratase activities, all compounds have inhibited the esterase activities of hCA I and II. The comparison of the inhibition studies of 1-5 to parent compounds indicates that 1-5 have superior inhibitory effects. The inhibition effects of 2-5 are also compared to inhibitory properties of the metal complexes of ABT and H(2)dipic, revealing an improved transfection profile.