Premium
Comparative studies on the interactions of baicalein and Al(III)–baicalein complex with human serum albumin
Author(s) -
Wang Jing,
Wang Qing,
Wu Di,
Yan Jin,
Wu You,
Li Hui
Publication year - 2016
Publication title -
luminescence
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.428
H-Index - 45
eISSN - 1522-7243
pISSN - 1522-7235
DOI - 10.1002/bio.2921
Subject(s) - baicalein , human serum albumin , fluorescence , circular dichroism , fourier transform infrared spectroscopy , förster resonance energy transfer , chemistry , fluorescence spectroscopy , nuclear chemistry , materials science , photochemistry , crystallography , chromatography , chemical engineering , genetics , physics , quantum mechanics , engineering , biology
A new potential drug aluminum(III)–baicalein complex (ALBC) was synthesized and characterized. The binding mechanisms of baicalein (BC) and ALBC to human serum albumin (HSA) under simulative physiological conditions were investigated, in order to understand the pharmacokinetics of BC and ALBC. Fluorescence spectroscopy results suggested that the binding level of BC is higher than that of ALBC. Results of UV–vis, synchronous fluorescence, 3D fluorescence, circular dichroism and Fourier transform infrared spectroscopic analyses consistently demonstrated that the conformation of HSA was altered when bound to BC or ALBC. The distance between HSA as a donor and BC (or ALBC) as an acceptor was determined via fluorescence resonance energy transfer. The results of competitive experiments and molecular docking studies indicated that BC was located in site I (subdomain IIA) on HSA and that ALBC was bound to HSA mainly within site II (subdomain IIIA). Copyright © 2015 John Wiley & Sons, Ltd.