Please use this identifier to cite or link to this item: https://scidar.kg.ac.rs/handle/123456789/13079
Title: Structural Characterization, Antimicrobial Activity and BSA/DNA Binding Affinity of New Silver(I) Complexes with Thianthrene and 1,8-Naphthyridine
Authors: Ašanin, Darko
Skaro Bogojevic, Sanja
Perdih, Franc
Andrejević, Tina
Milivojević, Dušan
Aleksic, Ivana
Nikodinovic-Runic, Jasmina
Glišić, Biljana
Turel, Iztok
Djuran, Miloš
Journal: Molecules (Basel, Switzerland)
Issue Date: 26-Mar-2021
Abstract: Three new silver(I) complexes [Ag(NO3)(tia)(H2O)]n (Ag1), [Ag(CF3SO3)(1,8-naph)]n (Ag2) and [Ag2(1,8-naph)2(H2O)1.2](PF6)2 (Ag3), where tia is thianthrene and 1,8-naph is 1,8-naphthyridine, were synthesized and structurally characterized by different spectroscopic and electrochemical methods and their crystal structures were determined by single-crystal X-ray diffraction analysis. Their antimicrobial potential was evaluated against four bacterial and three Candida species, and the obtained results revealed that these complexes showed significant activity toward the Gram-positive Staphylococcus aureus, Gram-negative Pseudomonas aeruginosa and the investigated Candida species with minimal inhibitory concentration (MIC) values in the range 1.56-7.81 μg/mL. On the other hand, tia and 1,8-naph ligands were not active against the investigated strains, suggesting that their complexation with Ag(I) ion results in the formation of antimicrobial compounds. Moreover, low toxicity of the complexes was detected by in vivo model Caenorhabditis elegans. The interaction of the complexes with calf thymus DNA (ct-DNA) and bovine serum albumin (BSA) was studied to evaluate their binding affinity towards these biomolecules for possible insights into the mode of antimicrobial activity. The binding affinity of Ag1-3 to BSA was higher than that for DNA, indicating that proteins could be more favorable binding sites for these complexes in comparison to the nucleic acids.
URI: https://scidar.kg.ac.rs/handle/123456789/13079
Type: Article
DOI: 10.3390/molecules26071871
SCOPUS: 85103863077
Appears in Collections:Faculty of Science, Kragujevac
Institute for Information Technologies, Kragujevac
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