albumin - publications

Predict more albumin - ligand interactions now!

1. Mol Biosyst. 2012 Feb 15. [Epub ahead of print]

Characterization of the interaction between nitrofurazone and human serum albumin
by spectroscopic and molecular modeling methods.

Deng F, Dong C, Liu Y.

College of Life and Environmental Science, Minzu University of China, Beijing
100081, People's Republic of China.

The interaction of nitrofurazone (NF) and human serum albumin (HSA) has been
studied by fluorescence spectroscopy, FT-IR spectroscopy and molecular modeling
methods. The results showed that the fluorescence of HSA was quenched by NF in a
static quenching mechanism. Thermodynamic parameters revealed that hydrogen bonds
and van der Waals force played the major role during the interaction. The
calculated binding distance (r) indicated that the non-radioactive energy
transfer came into being in the interaction between NF and HSA. HSA had a single
class of binding site at Sudlow' site I in subdomain IIA for NF, which was
verified by the displacement experiment. The molecular modeling study further
confirmed the specific binding sites of NF on HSA, such as the interaction
between N11 and N14 of NF with Lue 283 and Ser 287 predominately through hydrogen
bonds. Three-dimensional fluorescence spectra indicated that the polarity around
the tryptophan residues decreased and the conformation of HSA changed after
adding NF. FT-IR spectra showed that NF could induce the polypeptides of HSA
unfolding because it changed α-helix and β-sheet into β-turn and random structure
of HSA.

PMID: 22337082 [PubMed - as supplied by publisher]