albumin - publications

Predict more albumin - ligand interactions now!


1. Protein Pept Lett. 2012 Apr 18. [Epub ahead of print]

Study of the Interaction between Fisetin and Human Serum Albumin: A Biophysical
Approach.

Roy AS, Dinda AK, Dasgupta S.

Department of Chemistry, Indian Institute of Technology, Kharagpur-721302, India.
swagata@chem.iitkgp.ernet.in.

The binding of fisetin with human serum albumin (HSA) has been studied at
different pH using UV-Vis, FTIR, CD and fluorescence spectroscopic techniques.
The binding constants were found to increase with the rise in pH of the media.
The negative ∆H° (kJ/mol-1) and positive ∆S° (J/mol-1 K-1) indicate that fisetin
binds to HSA via electrostatic interactions with an initial hydrophobic
association that result in a positive ∆S°. In presence of potassium chloride
(KCl) the binding constants were found to be decrease. The α-helical content of
HSA increased after binding with fisetin as analyzed from both CD and FTIR
methods. The site marker displacement studies using fluorescence anisotropy
suggest that fisetin binds to the hydrophobic pocket (Site 1, subdomain IIA) of
HSA which is in good accordance with the molecular docking study. The change in
accessible surface area (ASA) of residues of HSA was calculated to get a better
insight into the binding.

PMID: 22519532 [PubMed - as supplied by publisher]