In:
Biological Chemistry, Walter de Gruyter GmbH, Vol. 391, No. 1 ( 2010-01-01)
Abstract:
Binding of fluorine-containing drugs to bovine β-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 β-lactoglobulin is folded and stable, were also studied, along with competition from molecules that can be regarded as analogs of physiological ligands to bovine β-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 β-lactoglobulin can bind and protect against low pH values various classes of drugs of pharmaceutical relevance.
Type of Medium:
Online Resource
ISSN:
1437-4315
,
1431-6730
Language:
Unknown
Publisher:
Walter de Gruyter GmbH
Publication Date:
2010
detail.hit.zdb_id:
1466062-3
SSG:
12