albumin - publications
Reviewing the binding of a series of parabens to human serum albumin.
Biopharm Drug Dispos. 2013 Jan 12;
Authors: Greige-Gerges H, Kaissi R, Magdalou J, Jraij A
To better understand the factors that contribute to the accumulation of unmetabolized parabens (p-hydroxybenzoic acid esters) in breast cancer tissue, we investigated the binding of a series of parabens (methyl-, ethyl-, butyl-, benzyl-paraben) to human serum albumin (HSA) by fluorescence spectroscopy and their ability to modify the binding parameters of albumin site markers. Emission spectra of HSA upon fluorescence excitation of Trp 214 residue at 295 nm were recorded at different molar ratios PB/HSA and data was corrected for the inner-filter effect. Significant inner-filter effect was obtained from molar ratios 2.0 and above. For lower molar ratios, a slight increase in fluorescence of HSA was detected. p-Hydroxybenzoic acid, the main metabolite of parabens, did not modify the fluorescence of HSA whatever the molar ratio used. Binding parameters for compounds that are markers of site I, bilirubin and warfarin, were determined in the absence and presence of methyl, butyl and benzyl paraben at molar ratios PB/HSA: 0, 1 and 2. No variation of the binding constants of these markers was observed. Our results indicate that parabens weakly interact with HSA thus suggesting that they are as a free form in blood and therefore more available to reach tissues. Copyright © 2013 John Wiley & Sons, Ltd.
PMID: 23315911 [PubMed - as supplied by publisher]