Title:Probing the Interaction of Anti-Cancer Agent Dihydromyricetin with Human Serum Albumin: A typical Method Study
Volume: 12
Issue: 8
Author(s): Tingting Chen, Shajun Zhu, Yapeng Lu, Hui Cao, Yu Zhao, Guoqing Jiang, Li Zhu and Tianhong Lu
Affiliation:
Keywords:
Dihydromyricetin, Human Serum Albumin, Interaction, Fluorescence, Circular dichroism, antioxidative, crystallographic, ligand, Sudlow I, DMY-HSA
Abstract: The interaction between dihydromyricetin (DMY) with human serum albumin (HSA) under the physiological conditions 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 bind to HSA with the binding affinities of the order 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.
