albumin - publications

Predict more albumin - ligand interactions now!

1. J Agric Food Chem. 2012 May 24. [Epub ahead of print]

Multi-spectroscopic and Molecular Modeling Approach to Investigate the
Interaction of Flavokawain B with Human Serum Albumin.

Feroz SR, Mohamad SB, Bujang N, Abd Malek SN, Tayyab S.

Interaction of flavokawain B (FB), a multi-therapeutic flavonoid from Alpinia
mutica with the major transport protein, human serum albumin (HSA) was
investigated using different spectroscopic probes, i.e. intrinsic, synchronous
and three-dimensional (3-D) fluorescence, circular dichroism (CD) as well as
molecular modeling studies. Values of binding parameters for FB-HSA interaction
in terms of binding constant and stoichiometry of binding were determined from
the fluorescence quench titration and were found to be 6.88 × 104 M-1 and 1.0
mole of FB bound per mole of protein, respectively, at 25°C. Thermodynamic
analysis of the binding data obtained at different temperatures showed that the
binding process was primarily mediated by hydrophobic interactions and hydrogen
bonding as the values of the enthalpy change (ΔH) and the entropy change (ΔS)
were found to be -6.87 kJ mol-1 and 69.50 J mol-1 K-1, respectively. FB binding
to HSA led to both secondary and tertiary structural alterations in the protein
as revealed by intrinsic, synchronous and 3-D fluorescence results. Increased
thermal stability of HSA in presence of FB was also evident from the far-UV CD
spectral results. The distance between the bound ligand and Trp-214 of HSA was
determined as 3.03 nm based on the Förster resonance energy transfer mechanism.
Displacement experiments using bilirubin and warfarin coupled with molecular
modeling studies assigned the binding site of FB on HSA at domain IIA, i.e.
Sudlow's site I.

PMID: 22624666 [PubMed - as supplied by publisher]