albumin - publications

Predict more albumin - ligand interactions now!

1. Talanta. 2012 Jan 15;88:524-32. Epub 2011 Nov 15.

Combined voltammetric and spectroscopic analysis of small molecule-biopolymer
interactions: The levodopa and serum albumin system.

Zhang Q, Ni Y, Kokot S.

State Key Laboratory of Food Science and Technology, Nanchang University,
Nanchang 330047, China.

An analytical method was researched for the simultaneous determination of
reactants and products during the binding of important small molecules such as
levodopa (LD) with biopolymers such as bovine serum albumin (BSA). Voltammetry
and fluorescence spectroscopy were used to obtain the analytical profiles from
different reactant mixtures as a function of concentration. This enabled the
extraction of the equilibrium constants (K(SV)) which are reported for the first
time. Voltammetric results supported the formation of the LD-BSA complex but not
that with dopamine. Further information of the LD-BSA system was unattainable
because the measured composite profiles could not be extracted. New information
was obtained when the extended data matrix was resolved by the MCR-ALS method.
The previously unavailable extracted voltammogram profile of LD-BSA complex
indicated that the complex was electroactive; this was unexpected if the LD-BSA
system was in its folded state, and hence, it was suggested that the protein must
be unfolded. The observation that the drug:BSA stoichiometry was 3:1, i.e.
(levodopa)(3)-BSA, supported this suggestion; these results were obtained from
the MCR-ALS extracted concentration profiles for the three reaction components.

Copyright © 2011 Elsevier B.V. All rights reserved.

PMID: 22265536 [PubMed - in process]