Spectroscopic Studies on the Interaction between Tilorone and Human Serum Albumin

Kashutskуy, Sergey

doi:10.17721/fujcV5I1P48-59

Spectroscopic Studies on the Interaction between Tilorone and Human Serum Albumin

Тип публікації :

Стаття

Дата випуску :

2017

Автор(и) :

Kashutskуy, Sergey

Мова основного тексту :

Англійська

eKNUTSHIR URL :

https://ir.library.knu.ua/handle/15071834/25555

DOI :

10.17721/fujcV5I1P48-59

Журнал :

French-Ukrainian Journal of Chemistry

Том :

5

Випуск :

1

ISSN :

2312-3222

Початкова сторінка :

48

Кінцева сторінка :

59

Цитування :

[APA 7] Kashutskуy, S. (2017). Spectroscopic Studies on the Interaction between Tilorone and Human Serum Albumin. French-Ukrainian Journal of Chemistry, 5(1), 48–59. https://doi.org/10.17721/fujcV5I1P48-59

[ДСТУ] Kashutskуy S. Spectroscopic Studies on the Interaction between Tilorone and Human Serum Albumin. French-Ukrainian Journal of Chemistry. 2017. Vol. 5, no. 1. P. 48—59. DOI: 10.17721/fujcV5I1P48-59 (date of access: 18.07.2026).

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.

Ключові слова :

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

Файл(и) :

Формат :

Adobe PDF

Розмір :

1.36 MB

Контрольна сума :

(MD5):1dab8613de76f18016baa93ad9655cde

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