albumin - publications

Predict more albumin - ligand interactions now!

1. Amino Acids. 2012 Feb 4. [Epub ahead of print]

Interactions of acidic pharmaceuticals with human serum albumin: insights into
the molecular toxicity of emerging pollutants.

Chen J, Zhou X, Zhang Y, Qian Y, Gao H.

Key Laboratory of Yangtze River Water Environment for Ministry of Education,
College of Environmental Science and Engineering, Tongji University, Shanghai,
200092, China.

Acidic pharmaceuticals such as diclofenac (DCF), clofibric acid (CA) and
ketoprofen (KTP) have been detected frequently in environmental media. In order
to reveal the toxicity of such emerging pollutants, their interactions with human
serum albumin (HSA) were investigated by capillary electrophoresis, molecular
spectrometry, and equilibrium dialysis. The binding constants and sites of these
acidic pharmaceuticals with HSA were obtained. The thermodynamic parameters, e.g.
enthalpy change and entropy change of these interactions were calculated to
characterize that all the reactions resulted from hydrophobic and electrostatic
interactions. The static quenching of the fluorescence of HSA was observed when
interacted with acidic pharmaceuticals, indicating acidic pharmaceuticals bound
to Tryptophan residue of HSA. The 3D fluorescence and circular dichroism
confirmed that the secondary conformation of HSA changed after the interactions
with the pharmaceuticals. At physiological condition, only 0.12 mM acidic
pharmaceuticals reduced the binding of vitamin B(2) to HSA by 37, 30 and 21% for
DCF, KTP and CA, respectively. This work provides an insight into non-covalent
interactions between emerging contaminants and biomolecule, and is helpful for
clarifying the toxic mechanism of such emerging contaminants.

PMID: 22307229 [PubMed - as supplied by publisher]