Synthesis and characterization of complexes of a novel proton transfer salt and their inhibition studies on carbonic anhydrase isoenzymes

Ilkimen H., Yenikaya C., SARI M., Bülbül M., Tunca E., DAL H., ...Daha Fazla

Journal of Enzyme Inhibition and Medicinal Chemistry, cilt.30, sa.2, ss.195-203, 2015 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 30 Sayı: 2
  • Basım Tarihi: 2015
  • Doi Numarası: 10.3109/14756366.2014.908290
  • Dergi Adı: Journal of Enzyme Inhibition and Medicinal Chemistry
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.195-203
  • Anahtar Kelimeler: 2-Amino-6-chlorobenzothiazole, 2,6-pyridinedicarboxylic acid, carbonic anhydrase, proton transfer, statistical analyses, DIPICOLINATE, BENZOXAZOLE, DERIVATIVES, ESTERASE
  • Anadolu Üniversitesi Adresli: Hayır

Özet

© 2014 Informa UK Ltd.A novel proton transfer compound (HClABT)+(HDPC.H2DPC)- (1) and its Fe(III), Co(II), Ni(II) and two different Cu(II) complexes (2-6) have been prepared and characterized by spectroscopic techniques. Additionally, single crystal X-ray diffraction techniques were applied to all complexes. All compounds, including acetazolamide (AAZ) as the control compound, were also evaluated for their in vitro inhibition effects on human hCA I and hCA 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 1-6 to parent compounds, ClABT and H2DPC, indicates that 1-6 have superior inhibitory effects. The inhibition effects of 2-6 are also compared to the inhibitory properties of the simple metal complexes of ClABT and H2DPC, revealing an improved transfection profile. Data have been analysed by using a one-way analysis of variance for multiple comparisons.