albumin - publications

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1. J Phys Chem B. 2012 May 21. [Epub ahead of print]

Complementary Fluorescence and Phosphorescence Study of the Interaction of
Brompheniramine with Human Serum Albumin.

Tardioli S, Lammers I, Hooijschuur JH, Ariese F, van der Zwan G, Gooijer C.

Binding of the antihistamine drug brompheniramine (BPA) to human serum albumin
(HSA) is studied by measuring quenching of the fluorescence and room temperature
phosphorescence (RTP) of tryptophan. The modified Stern-Volmer equation was used
to derive association constants and accessible fractions from the steady-state
fluorescence data. Decay associated spectra (DAS) revealed three tryptophan
fluorescence lifetimes, indicating the presence of three HSA conformations. BPA
causes mainly static quenching of the long-living, solvent-exposed conformer. RTP
spectra and lifetimes, recorded under deoxygenated conditions in the presence of
0.2 M KI, provided additional kinetic information about the HSA-BPA interactions.
Fluorescence DAS that were also recorded in the presence of 0.2 M KI, revealed
that the solvent-exposed conformer is the major contributor to the RTP signal.
The phosphorescence quenching is mostly dynamic at pH 7 and mostly static at pH
9, presumably related to the protonation state of the alkylamino chain of BPA.

PMID: 22612655 [PubMed - as supplied by publisher]