albumin - publications

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1. Int J Anal Chem. 2012;2012:408057. Epub 2012 Feb 20.

Interaction of avelox with bovine serum albumin and effect of the coexistent
drugs on the reaction.

Liu B, Yang C, Yan X, Wang J, Lv Y.

Key Laboratory of Medical Chemistry and Molecular Diagnosis, College of Chemistry
& Environmental Science, Hebei University, Ministry of Education, Baoding 071002,
China.

The interaction between Avelox and bovine serum albumin (BSA) was investigated at
different temperatures by fluorescence spectroscopy. Results showed that Avelox
could quench the intrinsic fluorescence of BSA strongly, and the quenching
mechanism was a static quenching process with Förester spectroscopy energy
transfer. The electrostatic force played an important role on the conjugation
reaction between BSA and Avelox. The order of magnitude of binding constants
(K(a)) was 10(4), and the number of binding site (n) in the binary system was
approximately equal to 1. The binding distance (r) was less than 3 nm and the
primary binding site for Avelox was located in subdomain IIA of BSA. Synchronous
fluorescence spectra clearly revealed that the microenvironment of amino acid
residues and the conformation of BSA were changed during the binding reaction. In
addition, the effect of some antibiotics on the binding constant of Avelox with
BSA was also studied.

PMCID: PMC3296219
PMID: 22505918 [PubMed - in process]