Abstract
The binding of L-tryptophan (L-Trp) and hesperidin (HES) was investigated by UV, fluorescence, synchronous fluorescence, time-resolved fluorescence, Fourier transform infrared (FTIR) spectroscopies, FRET, antibacterial activity, anticancer activity and molecular docking study. The flavonoid glycoside known as hesperidin has been shown to have therapeutic properties for a variety of disorders, including cancer diseases. Its low solubility and bioavailability cause it to be little absorbed, which means that a delivery mechanism is necessary in order for it to reach its therapeutic goal. Fluorescence data revealed that the fluorescence quenching mechanisms of L Trp by hesperidin are all static quenching procedures. Synchronous fluorescence spectroscopy shows the interaction between hesperidin and L-Trp changes the hydrophobicity of the microenvironment of tryptophan (Trp) residues. The anticancer activity effect of hesperidin and L-Trp on human cervical cancer cell lines was assessed using MTT and crystal violet assays.
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