Synthesis, biological and theoretical properties of crystal zinc complex with thiosemicarbazone of glyoxylic acid
JOURNAL OF MOLECULAR STRUCTURE, cilt.1248, 2022 (SCI-Expanded, Scopus)
- Yayın Türü: Makale / Tam Makale
- Cilt numarası: 1248
- Basım Tarihi: 2022
- Doi Numarası: 10.1016/j.molstruc.2021.131470
- Dergi Adı: JOURNAL OF MOLECULAR STRUCTURE
- Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, Chimica, Compendex, INSPEC
- Anahtar Kelimeler: Thiosemicarbazones, Synthesis, Crystal structure, Enzyme inhibition, Theoretical calculations, CARBONIC-ANHYDRASE, STRUCTURAL-CHARACTERIZATION, ANTIMICROBIAL ACTIVITIES, INHIBITORY PROPERTIES, METAL-COMPLEXES, HETEROCYCLIC THIOSEMICARBAZONES, COPPER(II) COMPLEXES, ACETYLCHOLINESTERASE, BUTYRYLCHOLINESTERASE, ANTIOXIDANT
- Marmara Üniversitesi Adresli: Evet
Özet
A new zinc complex with thiosemicarbazone of glyoxylic acid (1) was synthesized with zinc acetate dihy-drate and thiosemicarbazone of glyoxylic acid and crystallized in water. The absolute crystal structure of the complex was defined using the single-crystal X-ray diffraction technique. It was seen in X-ray mea-surements that the complex crystallized in the triclinic system with the P-1 space group. The structure of 1 represents distorted octahedral geometry around the central zinc metal. Zn(II) complex with thiosemi-carbazone of glyoxylic acid was an inhibitor of acetylcholinesterase (AChE), butyrylcholinesterase (BChE), human carbonic anhydrase I and II isoforms (hCA I and II) receptors and the inhibitor constant (Ki) values of the synthesized complex were 38.94 +/- 8.2 mu M for hCA I, 48.62 +/- 11.3 mu M for hCA II, 65.16 +/- 11.4 mu M for BChE and 82.04 +/- 16.0 mu M for AChE, respectively. The molecular docking method was used to show the complex-enzyme interactions. The pharmacokinetic properties of the complex were determined by ADME/Tox predictions and the results obtained showed that the complex could be a potential drug can-didate. (C) 2021 Elsevier B.V. All rights reserved.