Spectroscopic Studies on the Interaction between Tilorone and Human Serum Albumin

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

Abstract


Under physiological conditions, in vitro interaction between the antiviral drug 2,7-bis[2-(diethylamino)ethoxy]-9-fluorenone dihydrochloride (Tilorone, TIL) and human serum albumin (HSA) was investigated at excitation wavelength 280 nm and at different temperatures (298 K and 313 K) by fluorescence emission spectroscopy. TIL showed a strong ability to quench the intrinsic fluorescence of HSA through a static quenching procedure. The binding constant is estimated as KA =7.19× 104L·mol-1 at 298 K. The enthalpy change (ΔHº) and entropy change (ΔSº) were derived to be negative values. A value of 1.63 nm for the average distance r between TIL (acceptor) and tryptophan residues of HSA (donor) was derived from the fluorescence resonance energy transfer.


Keywords


fluorenone; human serum albumin; fluorescence quenching; fluorescence resonance energy transfer; thermodynamic parameters

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DOI: https://doi.org/10.17721/fujcV5I1P48-59

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