Novel zinc compound with thiosemicarbazone of glyoxylic acid: Synthesis, crystal structure, and bioactivity properties

被引:9
|
作者
Huseynova, Mansura [1 ]
Farzaliyev, Vaqif [1 ]
Medjidov, Ajdar [2 ]
Aliyeva, Mahizar [1 ]
Taslimi, Parham [3 ]
Sahin, Onur [4 ]
Yalcin, Bahattin [5 ]
机构
[1] Natl Acad Sci, Inst Chem Addit, Bigshor Highway,Block 2062, AZ-1029 Baku, Azerbaijan
[2] Natl Acad Sci, Inst Catalysis & Inorgan Chem, H Cavid Ave 113, AZ-1143 Baku, Azerbaijan
[3] Bartin Univ, Fac Sci, Dept Biotechnol, TR-74100 Bartin, Turkey
[4] Sinop Univ, Sci & Technol Res Applicat & Res Ctr, TR-57000 Sinop, Turkey
[5] Marmara Univ, Fac Arts Sci, Dept Chem, TR-81040 Istanbul, Turkey
关键词
Zn-complex; Thiosemicarbazones; Crystal structure; Enzyme inhibition; CARBONIC-ANHYDRASE; BIOLOGICAL-ACTIVITY; HETEROCYCLIC THIOSEMICARBAZONES; INHIBITORY PROPERTIES; METAL-COMPLEXES; 3-AMINOPYRIDINE-2-CARBOXALDEHYDE THIOSEMICARBAZONE; RIBONUCLEOTIDE REDUCTASE; COPPER(II) COMPLEXES; MULTIDRUG-RESISTANCE; ANTITUMOR-ACTIVITY;
D O I
10.1016/j.molstruc.2019.127082
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
Reaction of zinc nitrate with thiosemicarbazone of glyoxylic acid (H(2)GAT) leads to the formation of the new complex that have been characterized by spectroscopic methods. Crystal structure of the compound Zn3C18H34N18O17S6 (1) was determined using single crystal X-ray diffraction methods. Single crystal X-ray measurements showed that the complex crystallized in a triclinic system with the space group P-1. The structure of complex 1 presents distorted octahedral geometry around the zinc ion centre. In the crystal structure, Zn(II) ion is coordinated by two nitrogen, two oxygen and two sulfur atoms from two different thiosemicarbazone of glyoxylic acid and two oxygen atoms from two different water molecules. Thermogravimetry shows four steps of decomposition in the temperature range 225-990 degrees C. This complex was an inhibitor of butyrylcholinesterase (BChE), cytosolic carbonic anhydride I and II isoforms (hCA I and II) and acetylcholinesterase (AChE) enzymes for complex 1 with Ki values of 0.95 +/- 0.10 mu M for hCA I, 1.54 +/- 0.24 mu M for hCA II, 25.98 +/- 2.44 mu M for BChE, 166.21 +/- 13.63 mu M for alpha-glycosidase and 18.53 +/- 1.36 mu M for AChE, respectively. (C) 2019 Elsevier B.V. All rights reserved.
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页数:9
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