Please use this identifier to cite or link to this item:
Title: New mononuclear gold(III) complexes: Synthesis, characterization, kinetic, mechanistic, DNA/BSA/HSA binding, DFT and molecular docking studies
Authors: Radisavljević, Snežana
Scheurer A.
Bockfeld, Dirk
Ćoćić, Dušan
Puchta, Ralph
Senft L.
Pešić, Marko
Damljanović, Ivan
Petrović, Biljana
Issue Date: 2021
Abstract: Five new gold(III) complexes, with general formula [Au(N[sbnd]N)Cl2]+ for complexes 1–3 and [Au(N[sbnd]N)2]3+ for complexes 4–5 (where N[sbnd]N is 3-((2-((5-phenyl-1H-pyrazol-3-yl)methoxy)naphthalene-3-yloxy)methyl)-5-phenyl-1H-pyrazole – L1, (3-((2-((5-phenyl-1H-pyrazol-3-yl)methoxy) phenoxy)methyl)-5-phenyl-1H-pyrazole – L2, (3-((2-((5-naphthalen-2-yl)-1H-pyrazol-3-yl)methoxy)phenoxy)methyl)-5-(naphthalen-3-yl)-1H-pyrazole – L3), were synthesized and characterized by elemental analysis, 1H NMR, IR, UV–Vis, ESI-MS and conductometry. Also, ligand L2 was characterized by X-ray analysis. Stability of complexes in water and in Hepes buffer was confirmed by UV–Vis. Kinetics and mechanism of the substitution reactions of 1–3 with guanosine-5′-monophosphate (5′-GMP), glutathione (GSH) and. L-Methionine (L-Met) were studied by stopped-flow technique. Obtained results have shown that complex 1 is the most reactive, while the reactivity of the nucleophiles decreases in order: GSH > 5′-GMP > L-Met. Calculated values of the entropy of activation support an associative mechanism. Redox stability of complexes 1–3 was investigated in the presence of the same biomolecules by cyclic voltametry. Obtained voltammograms showed reduction of gold(III) up to gold(0). DNA binding studies in the presence of ethidium bromide (EB) and 2-(4-hydroxyphenyl)-5-[5-(4-methylpipera-zine-1yl)-benzimidazo-2-yl]-benzimidazole (HOE) were performed by UV–Vis, fluorescence spectroscopy and viscosity measurements, in order to assess the binding mode. The results showed that gold(III) complexes interact with calf-thymus (CT-DNA) via covalently binding mode rather than via intercalation. Also, all complexes shown high values of binding constants for the interactions with bovine serum albumin (BSA) and human serum albumin (HSA). Furthermore, the binding studies with CT-DNA and BSA/HSA were supported by molecular docking. The strong connection between structure and reactivity of gold(III) complexes toward biologically important molecules was confirmed.
Type: article
DOI: 10.1016/j.poly.2021.115446
ISSN: 0277-5387
SCOPUS: 2-s2.0-85114165575
Appears in Collections:Faculty of Science, Kragujevac

Page views(s)




Files in This Item:
File Description SizeFormat 
  Restricted Access
29.86 kBAdobe PDFThumbnail

Items in SCIDAR are protected by copyright, with all rights reserved, unless otherwise indicated.