Supramolecular complexes of Ni (II) and Co (II) 4-aminobenzoate with 3-cyanopyridine: Synthesis, spectroscopic characterization, crystal structure, and enzyme inhibitory properties


SERTÇELİK M., ÖZBEK F. E., Taslimi P., NECEFOĞLU H., HÖKELEK T.

APPLIED ORGANOMETALLIC CHEMISTRY, cilt.35, sa.5, 2021 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 35 Sayı: 5
  • Basım Tarihi: 2021
  • Doi Numarası: 10.1002/aoc.6182
  • Dergi Adı: APPLIED ORGANOMETALLIC CHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, Aerospace Database, BIOSIS, Chemical Abstracts Core, Chimica, Communication Abstracts, Compendex, Metadex, DIALNET, Civil Engineering Abstracts
  • Anahtar Kelimeler: 3&#8208, cyanopyridine, 4&#8208, aminobenzoate, metabolic enzyme inhibition, Ni and co complex, XRD, PARA-AMINOBENZOIC ACID, CARBONIC-ANHYDRASE, DERIVATIVES, ACETYLCHOLINESTERASE, THIOSEMICARBAZONE, CHOLINESTERASE, ANTIBACTERIAL, IMIDAZOLINIUM, ANTICANCER, POLYMER
  • Hacettepe Üniversitesi Adresli: Evet

Özet

Two new complexes, [M (AB)(2)(CP)(2)(H2O)(2)] (where M = Ni and Co AB = 4-aminobenzoate and CP = cyanopyridine), were synthesized and characterized using different techniques (elemental analysis, FT-IR spectrophotometer, LC/MS, single-crystal X-ray diffraction, and TGA/DTA analysis). As a result of X-ray structural analysis, it was determined that complexes are isostructural. In the crystalline structures, M-II ions are bridged with their carboxylate oxygen and aminopyridine nitrogen atoms and their symmetry-related counterparts to form a two-dimensional polymeric structure. The M-II ion is octa-coordinated with two nitrogen atoms and two oxygen atoms of the AB and two atoms of the CP anions. In this study, the effect of these molecules, containing a biologically active group, was investigated on important metabolic enzymes (carbonic anhydrase isoenzymes I and II (hCA I and II), achethylcholinesterase (AChE), and alpha-glycosidase (alpha-Gly) enzymes).