Spectroscopic Studies on the Interaction Between Novel Antiviral Drug Favipiravir and Serum Albumins

Alla Yegorova, Yulia Scrypynets, Georgy Maltsev, Inna Leonenko, Valery Antonovich, Sergey Kashutskуy, Olga Voitiuk


Under physiological conditions, in vitro interaction between favipiravir (FAV) and serum albumins (BSA/HSA) was investigated at excitation wavelength 280 nm and at different temperatures (298 K, 313 K) by fluorescence emission spectroscopy. The hydrogen bond, van der Waals forces and electrostatic interaction plays a major role in stabilizing the complex; the binding constants KA at different temperatures were calculated. The distance r between donor (BSA/HSA) and acceptor (FAV) was obtained according to fluorescence resonance energy transfer (1.55/1.90 nm for BSA/HSA-FAV systems). The effect of FAV on the conformation of BSA/HSA was analyzed using synchronous fluorescence spectroscopy and UV/vis absorption spectroscopy.


favipiravir; serum albumin; protein-ligand interaction; fluorescence quenching; fluorescence resonance energy transfer; thermodynamic parameters

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