NDLI: Studies of the interaction between apigenin and bovine serum albumin by spectroscopic methods

Content Provider	Springer Nature Link
Author	Shang, Yonghui Li, Hua
Copyright Year	2010
Abstract	The interaction between apigenin (Ap) and bovine serum albumin (BSA) in physiological buffer (pH = 7.4) is investigated by fluorescence quenching technique and UV-vis absorption spectra. The results reveal that Ap could strongly quench the intrinsic fluorescence of BSA. The quenching mechanism of Ap for BSA varies with the change of Ap concentration. when Ap concentration is lower, it is a static quenching procedure, when Ap concentration is higher, a combined quenching (both static and dynamic) would operate. The apparent binding constants Ka and number of binding sites n of Ap with BSA are obtained by fluorescence quenching method. The thermodynamic parameters, enthalpy change (Δ$_{r}$ H $^{m}$ and entropy change (Δ$_{r}$ S $^{m}$), are calculated to be −15.382 kJ mol$^{−1}$ K$^{−1}$ < 0 and 104.888 J mol$^{−1}$ K$^{−1}$ > 0, respectively, which indicate that the interaction of Ap with BSA is driven mainly by hydrogen bonding and hydrophobic interactions. The distance r between BSA and Ap is calculated to be 1.89 nm based on Förster’s non-radiative energy transfer theory. The results of synchronous fluorescence spectra show that binding of Ap with BSA cannot induce conformational changes in BSA.
Starting Page	1710
Ending Page	1717
Page Count	8
File Format	PDF
ISSN	10703632
Journal	Russian Journal of General Chemistry
Volume Number	80
Issue Number	8
e-ISSN	16083350
Language	English
Publisher	SP MAIK Nauka/Interperiodica
Publisher Date	2010-09-22
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Chemistry/Food Science
Content Type	Text
Resource Type	Article
Subject	Chemistry

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