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Protein interactions, molecular docking, antimicrobial and antifungal studies of terpyridine ligandsBehera, S.; Dash, Pragyan P.; Bishoyi, Ajit K.; Dash, K.; Mohanty, P.; Sahoo, Chita R.; Padhy, Rabindra N.; Mishra, M.; Ghosh, B. N.; Sahoo, H.; Jali, B. R.
Journal of biomolecular structure & dynamics, 12/2023, Letnik: ahead-of-print, Številka: ahead-of-printJournal Article
Resistance to antibiotics/antibacterials/antifungals in pathogenic microbes has been developing over the past few decades and has recently become a commonplace public-health peril. Thus, alternative nontoxic potent antibiotic agents are covertly needed to control antibiotic-resistant outbreaks. In an effort to combat the challenges posed by the co-occurrence of multidrug resistance, two terpyridine ligands 4′-(4-N,N′-dimethylaminophenyl)-2,2′:6′,2″-terpyridine (L1) and 4′-(4-tolyl)-2,2′:6′,2″-terpyridine (L2) have been designed, prepared and confirmed their structure by spectral studies. Thereafter, antimicrobial assay was performed against gram positive and negative bacterial strains along with fungal strains. Both compounds L1 and L2 exhibited remarkable inhibitory activities against bacteria, Escherichia coli and Staphylococcus aureus at MIC values 6.25 and 3.125 µg/ml, respectively. In addition, in silico molecular docking studies were ascertained with bacterial DNA gyrase and fungal demethylase. Furthermore, both L1 and L2 could bind Bovine Serum Albumin (BSA) protein and binding interaction has been studied with the help of UV-Visible and fluorescence spectroscopy. While fluorescence of BSA unperturbed in the presence of L2, an addition of L1 to the solution of BSA resulted significant quenching. The binding constant calculations at different temperature confirmed that the fluorescence quenching between BSA and L1 is predominantly static in nature. The toxicity of L1 and L2 was checked using Drosophila melanogaster. The toxicity analysis suggest both the dyes are non-cytotoxic in nature. Communicated by Ramaswamy H. Sarma
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