albumin - publications

Predict more albumin - ligand interactions now!

1. J Agric Food Chem. 2012 Feb 21. [Epub ahead of print]

Probing the binding of the flavonoid diosmetin to human serum albumin by
multi-spectroscopic techniques.

Zhang G, Wang L, Pan J.

The binding mechanism of molecular interaction between diosmetin and human serum
albumin (HSA) in a pH 7.4 phosphate buffer was studied using atomic force
microscopy (AFM) and various spectroscopic techniques including fluorescence,
resonance light scattering (RLS), UV-vis absorption, circular dichroism (CD) and
Fourier transform infrared (FT-IR) spectroscopy. Fluorescence data revealed that
the fluorescence quenching of HSA by diosmetin was a static quenching procedure.
The binding constants and number of binding sites were evaluated at different
temperatures. The RLS spectra and AFM images showed that the dimension of the
individual HSA molecules were larger after interaction with diosmetin. The
thermodynamic parameters, ΔH° and ΔS° were calculated to be -24.56 kJ mol-1 and
14.67 J mol-1 K-1, respectively, suggesting that the binding of diosmtin to HSA
was driven mainly by hydrophobic interactions and hydrogen bonds. The
displacement studies and denaturation experiments in the presence of urea
indicated the site I as the main binding site for diosmetin on HSA. The binding
distance between diosmetin and HSA was determined to be 3.54 nm based on the
Förster theory. Analysis of CD and FT-IR spectra demonstrated that HSA
conformation was slightly altered in the presence of diosmetin.

PMID: 22353148 [PubMed - as supplied by publisher]