albumin - publications

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1. J Pharm Biomed Anal. 2012 Mar 15. [Epub ahead of print]

Comparative studies on the interactions of honokiol and magnolol with human serum
albumin.

Cheng Z.

Chemical Synthesis and Pollution Control Key Laboratory of Sichuan Province,
China West Normal University, Nanchong 637002, China.

In this study, the binding modes of honokiol (HK) and magnolol (MG) with human
serum albumin (HSA) have been established under imitated physiological condition,
which was very important to understand the pharmacokinetics and toxicity of HK or
MG. The experimental results proved that the fluorescence of HSA was quenched by
HK or MG through a static quenching procedure. The binding constants of HK-HSA
and MG-HSA complexes were 5.304 and 263.755×10(4)Lmol(-1) at 298K, respectively.
The binding process was a spontaneous molecular interaction procedure, in which
the hydrophobic interaction played a major role in the formation of the HK-HSA
complex, whereas, the binding interaction between MG and HSA might involve the
hydrophobic interaction strongly and electrostatic interaction. In addition, the
effect of HK/MG on the secondary structure of HSA was analyzed using CD, UV-vis
absorption, Fourier transform infrared (FT-IR), synchronous fluorescence and
three-dimensional fluorescence spectra. According to Förster no-radiation energy
transfer theory, the binding distance of HSA to HK or MG was calculated to be
1.842 or 1.238nm. Besides, the effects of common ions on the binding constants of
HSA-HK/MG systems were also discussed.

Copyright © 2012 Elsevier B.V. All rights reserved.

PMID: 22480476 [PubMed - as supplied by publisher]