(2019) Novel tetradentate Schiff base zinc(II) complex as a potential antioxidant and cancer chemotherapeutic agent: Insights from the photophysical and computational approach. Journal of Molecular Structure. pp. 536-544. ISSN 0022-2860
Full text not available from this repository.
Abstract
In this study a new N4 Schiff base ligand (SB) was synthesized via condensation reaction of 3,4-diaminobenzophenone with diacetyl monoxime in 1:2 M ratio. Moreover, the synthesization and characterization of its zinc (II) complex was carried out through elemental analysis, FT-IR, H-1 NMR, UV-Vis spectroscopies and molar conductance. Afterwards we scrutinized the above obtained complex to determine its potential anticancer activity against MCF-7 cell line through MTT test, reducing the viable cell numbers to 11 of the control samples after exposure for 72 h. In order to specify its in vitro antioxidant activity, the Zn(II) complex was evaluated, as a radical scavenger, versus 1,1-diphenyl-2-picrylhydrazyl radicals (DPPH center dot). Data obtained from the above assay revealed that Zn(II) complex demonstrated limited (IC50 = 239.5 mgL(-1)) antioxidant activity in comparison with ascorbic acid. For the purpose of investigating the complex-model proteins binding, human serum albumin (HSA) and beta-lactoglobulin (beta-LG), we used biophysical methods and molecular modeling. Experimental results showed that the two systems demonstrated identical interactions (hydrogen bonding and Van der Waals forces). But the beta-LG demonstrated a much firmer binding affinity to Zn(II) complex than HSA (K-b similar to 0.67 (+/- 0.10) x 10(4) M-1 for HSA-Zn complex and 6.45 (+/- 0.15) x 104 M-1 for beta-LG-Zn complex). According to the molecular modeling analysis, the Zn(II) complex develops bonds to the remnants that exist in the subdomain HA of HSA and site A of beta-LG. (C) 2018 Elsevier B.V. All rights reserved.
Item Type: | Article |
---|---|
Keywords: | Schiff base complex Antioxidant Anti-cancer Protein interaction human serum-albumin crystal-structure oxali-palladium binding docking site tamoxifen zn(ii) ligand Chemistry |
Divisions: | |
Page Range: | pp. 536-544 |
Journal or Publication Title: | Journal of Molecular Structure |
Volume: | 1177 |
Identification Number: | 10.1016/j.molstruc.2018.10.005 |
ISSN: | 0022-2860 |
Depositing User: | مهندس مهدی شریفی |
URI: | http://eprints.zbmu.ac.ir/id/eprint/3721 |
Actions (login required)
View Item |