Copper complexes containing thiosemicarbazones derived from 6-nitropiperonal: Antimicrobial and biophysical properties.

Autor: Beckford FA; Department of Natural Sciences, The University of Virginia's College at Wise, 1 College Avenue, Wise, VA 24293, United States. Electronic address: fab5b@uvawise.edu., Webb KR; Department of Natural Sciences, The University of Virginia's College at Wise, 1 College Avenue, Wise, VA 24293, United States.
Jazyk: angličtina
Zdroj: Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy [Spectrochim Acta A Mol Biomol Spectrosc] 2017 Aug 05; Vol. 183, pp. 158-171. Date of Electronic Publication: 2017 Apr 20.
DOI: 10.1016/j.saa.2017.04.057
Abstrakt: A series of four thiosemicarbazones from 6-nitropiperonal along with the corresponding copper complexes were synthesized. The biophysical characteristics of the complexes were investigated by the binding to DNA and human serum albumin. The binding to DNA is moderate; the binding constants run from (0.49-7.50)×10 4 M -1 . In relation to HSA, the complexes interact strongly with binding constants on the order of 10 5 M -1 . The complexes also display antioxidant behavior as determined by the ability to scavenge diphenylpicrylhydrazyl (dpph) and nitric oxide radicals. The antimicrobial profiles of the compounds, tested against a panel of microbes including five of the ESKAPE pathogens (Staphylococcus aureus, MRSA, Escherichia coli, Klebsiella pneumoniae, MDR, Acinetobacter baumannii, Pseudomonas aeruginosa) and two yeasts (Candida albicans and Cryptococcus neoformans var. grubii), are also described. The compounds contain a core moiety that is similar to oxolinic acid, a quinolone antibiotic that targets DNA gyrase and topoisomerase (IV). The binding interaction between the complexes and these important antibacterial targets were studied by computational methods, chiefly docking studies. The calculated dissociation constants for the interaction with DNA gyrase B (from Staphylococcus aureus) range from 4.32 to 24.65μM; the binding was much stronger to topoisomerase IV, with dissociation constants ranging from 0.37 to 1.27μM.
(Copyright © 2017 Elsevier B.V. All rights reserved.)
Databáze: MEDLINE
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