Journal
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 57, Issue -, Pages 226-231Publisher
ELSEVIER
DOI: 10.1016/j.ijbiomac.2013.03.021
Keywords
Bovine beta-lactoglobulin; Oleic acid; Linoleic acid; Crystal structure; Isothermal titration calorimetry
Funding
- Polish Ministry of Science and Higher Education [3240/B/H03/2009/37 (N N204 324037)]
- European Regional Development Fund in the framework of the Polish Innovation Economy Operational Program [POIG.02.01.00-12-023/08]
- Bleriot scholarship from Region Nord Pas de Calais, France
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Binding of 18-carbon unsaturated oleic and linoleic acid to lactoglobulin, the milk protein, has been studied for the first time by isothermal titration calorimetiy (ITC) and X-ray crystallography. Crystal structures determined to resolution 2.10 angstrom have revealed presence of single fatty acid molecule bound in beta-barrel, the primary binding site, with carboxyl group hydrogen bonded to Glu62. The aliphatic chain of both ligands is in almost linear conformation and their interactions with the protein are similar to observed in structure of lactoglobulin with stearic acid. The ITC experiments showed that binding of unsaturated fatty acids to LGB is spontaneous and exothermic. The stoichiometry of binding is lower than 1.0, association constant is 9.7 x 10(5) M-1 and 9.0 x 10(5) M-1 for oleic and linoleic acid, respectively. Solvent relief seems to be the major contributor to entropic changes upon fatty acid binding to lactoglobulin. (c) 2013 Elsevier B.V. All rights reserved.
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