Spectroscopic Studies on the Interaction between Tilorone and Human Serum Albumin

Authors

  • Alla Yegorova A.V. Bogatsky Physico-chemical Institute of the National Academy of Sciences of Ukraine
  • Inna Leonenko A.V. Bogatsky Physico-chemical Institute of the National Academy of Sciences of Ukraine
  • Yulia Scrypynets A.V. Bogatsky Physico-chemical Institute of the National Academy of Sciences of Ukraine
  • Georgy Maltsev Open Joint-Stock Ukrainian - Belgian Chemical Enterprise " InterChem ", Lustdorfskaya doroga 86, Odessa 65080, Ukraine
  • Valery Antonovich A.V. Bogatsky Physico-chemical Institute of the National Academy of Sciences of Ukraine
  • Sergey Kashutskуy Open Joint-Stock Ukrainian - Belgian Chemical Enterprise " InterChem ", Lustdorfskaya doroga 86, Odessa 65080, Ukraine

DOI:

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

Keywords:

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

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.

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Published

2017-05-10

Issue

Vol. 5 No. 1 (2017)

Section

Articles

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