albumin - publications

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1. J Photochem Photobiol B. 2012 Jan 20. [Epub ahead of print]

Spectroscopic, structural and thermodynamic properties of chlorpyrifos bound to
serum albumin: A comparative study between BSA and HSA.

Han XL, Tian FF, Ge YS, Jiang FL, Lai L, Li DW, Yu QL, Wang J, Lin C, Liu Y.

State Key Laboratory of Virology & Key Laboratory of Analytical Chemistry for
Biology and Medicine (Ministry of Education), College of Chemistry and Molecule
Sciences, Wuhan University, Wuhan 430072, PR China.

Chlorpyrifos (CPF) is a widely used organophosphate insecticide which could bind
with human serum albumin (HSA) and bovine serum albumin (BSA). The binding
behavior was studied employing fluorescence, three-dimensional fluorescence,
Circular dichroism (CD) spectroscopy, UV-vis absorption spectroscopy,
electrochemistry and molecular modeling methods. The fluorescence spectra
revealed that CPF causes the quenching of the fluorescence emission of serum
albumin. Stern-Volmer plots were made and quenching constants were thus obtained.
The results suggested the formation of the complexes of CPF with serum albumins,
which were in good agreement with the results from electrochemical experiments.
Association constants at 25°C were 3.039×10(5)molL(-1) for HSA, and
0.3307×10(5)molL(-1) for BSA, which could affect the distribution, metabolism,
and excretion of pesticide. The alterations of protein secondary structure in the
presence of CPF were confirmed by the evidences from UV and CD spectra. Site
competitive experiments also suggested that the primary binding site for CPF on
serum albumin is close to tryptophan residues 214 of HSA and 212 of BSA, which
was further confirmed by molecular modeling.

Copyright © 2012 Elsevier B.V. All rights reserved.

PMID: 22316628 [PubMed - as supplied by publisher]