albumin - publications

Predict more albumin - ligand interactions now!


1. Anticancer Agents Med Chem. 2012 Jan 31. [Epub ahead of print]

Probing the Interaction of Anti-cancer agent Dihydromyricetin with Human Serum
Albumin: A typical method study.

Chen T, Zhu S, Lu Y, Zhao Y, Jiang G, Zhu L, Lu T.

Nantong University, Nantong, 226019, P. R. China. lzhu1965@yahoo.com.cn (L. Zhu).

The interaction between dihydromyricetin (DMY) with human serum albumin (HSA)
under the physiological condition was investigated by fluorescence spectroscopy,
circular dichroism (CD) spectra and UV-visible absorption spectroscopy. In the
mechanism discussion it was proved that the fluorescence quenching of HSA by DMY
is a result of the formation of DMY-HSA complex. Binding parameters calculated
showed that DMY was bound to HSA with the binding affinities of 105~106 L·mol-1.
The enthalpy change (ΔH) and entropy change (ΔS) were calculated to be -28.76
kJ·mol-1 and 18.21 J·mol-1·K-1, respectively, which implied that the hydrophobic
and hydrogen bonds interactions play predominant roles in the binding process.
The binding site of DMY on HSA may be located in hydrophobic cavity of subdomain
IIA by the analysis data of fluorescence and synchronous fluorescence spectra.
The specific binding distance r (3.37 nm) between donor (Trp-214) and acceptor
(DMY) was obtained according to Förster non-radiative resonance energy transfer
theory. CD spectral result demonstrates that DMY does not affect the secondary
structure of HSA and can maintain protein stabilization. In addition, the effect
of some common metal ions (e.g. Zn2+, Cu2+, Co2+, Ni2+, Fe3+) on the binding
constant between DMY and HSA was examined.

PMID: 22292768 [PubMed - as supplied by publisher]