Bovine beta-lactoglobulin acts as an acid-resistant drug carrier by exploiting its diverse binding regions

Biological Chemistry
Alberto BarbiroliMaria Caterina Vilardo

Abstract

Binding of fluorine-containing drugs to bovine beta-lactoglobulin, the most abundant whey protein in bovine milk, was investigated by means of (19)F NMR and mass spectrometry. The stoichiometry of the binding and its stability in acidic medium, where beta-lactoglobulin is folded and stable, were also studied, along with competition from molecules that can be regarded as analogs of physiological ligands to bovine beta-lactoglobulin. Conditional binding data were combined with protein structural information derived from circular dichroism and limited proteolysis studies. Spectroscopic techniques were also used to assess whether the bound drugs stabilize the protein structure against denaturation by chaotropes or temperature at various pH values. The results obtained provide evidence for the presence of multiple binding regions on the protein, with a specific and different affinity for structurally different classes of hydrophobic drugs and, more generally, that bovine beta-lactoglobulin can bind and protect against low pH values various classes of drugs of pharmaceutical relevance.

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Citations

May 27, 2011·Amino Acids·Ivano EberiniElisabetta Gianazza
Sep 17, 2015·Journal of Biomolecular Structure & Dynamics·Martiniano Bello
Sep 29, 2011·Molecular Nutrition & Food Research·Mauro MarengoHanne Frokiaer
Jul 15, 2015·PloS One·Tiziana BeringhelliIvano Eberini
Dec 14, 2016·BioMed Research International·Chun San TaiWen Liang Chen
Mar 30, 2019·European Biophysics Journal : EBJ·Lilia AnghelRaul Victor Erhan
Oct 30, 2010·Journal of Agricultural and Food Chemistry·Tiziana Mariarita GranatoFrancesco Bonomi
Apr 22, 2011·Journal of Agricultural and Food Chemistry·Alberto BarbiroliStefania Iametti
Mar 20, 2012·International Journal of Biological Macromolecules·Joanna I LochKrzysztof Lewiński

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