1,2,3-triazole hybrid organosilanes: Synthesis, photophysical detection of F- ions and molecular docking.

This paper represents the synthesis of 1,2,3-triazole hybrid organosilanes as sensors for the detection of F- ions, antibacterial activity and molecular docking analysis in the active sites of DNA gyrase of S. aureus (5CPH). Further, the binding mode of compound 7a with F- was proven by Density functional theory (DFT) calculations. [Display omitted] • 1,2,3-triazole hybrid organosilanes have been synthesized and characterized. • Sensing behavior of the organosilanes were evaluated towards various ions. • The binding mode of compound 7a with F- was proven by DFT calculations. • The prepared compounds showed inhibitory activity against Staphylococcus aureus. • Molecular docking was performed for compound 7a with the active sites of 5CPH. Among various anions, fluoride is one of the most essential because of its use in the treatment of osteoporosis and dental care, but excessive use can have negative effects on human health. Owing to these reasons, the present study addresses the efficient synthesis of 1,2,3-triazole hybrid organosilanes achieved via a copper-catalyzed azide–alkyne cycloaddition (CuAAC) click chemistry followed by the condensation reaction. The synthesized compounds were confirmed by (1H and 13C) NMR spectroscopy and mass spectrometry. The compounds 7a-7b showed high selectivity and sensitivity toward F- ions with limit of detection (LOD) of 1.11 × 10-6 M and 43 × 10-6 M respectively. The binding mode of compound 7a with F- was proven by Density functional theory (DFT) calculations. The in vitro antibacterial activity of synthesized compounds 7a-7b against two gram-negative (Escherichia coli and Pseudomonas aeruginosa) and one gram-positive (Staphylococcus aureus) bacterial strains were determined, and the results exhibited good inhibitory activity against gram-positive (Staphylococcus aureus). Additionally, molecular docking study was carried out to look into the interaction between compound 7a and the active sites of the S. aureus DNA gyrase (5CPH). The docking results revealed the better affinity for protein with binding energy of −6.55 kcal/mol. [ABSTRACT FROM AUTHOR]