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Interactions of β-Lactoglobulin Variants A and B with Vitamin A. Competitive Binding of Retinoids and Carotenoids

Abstract : beta-Lactoglobulin (beta-Lg) is the major whey protein -of bovine milk present at a concentration of 2-3 g L-1. Its biological role is still not well-known. However, many studies have suggested that beta-Lg may play either nutritional or specific transporter role. The high affinity of beta-Lg for retinol and other retinoids was reported. The results of interaction studies of beta-Lg with carotenoids, that is, beta-carotene, beta-cryptoxanthin, and alpha-carotene, which display similar structures are reported in this study. The affinities of beta-Lg for binding of retinoids and carotenoids were compared, providing more information about the binding site(s) of these molecules by beta-Lg. Interactions were followed by the measurements of quenching of beta-Lg tryptophan fluorescence and retinol fluorescence. The obtained results indicate that carotenoids are bound by beta-Lg with high affinity of the order of 10(-8) M. Measurement of retinol competition with carotenoids for binding by beta-Lg suggests that the binding of these two ligands occurs at two different sites of beta-Lg.
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https://www.hal.inserm.fr/inserm-01478545
Contributor : Patrick Borel <>
Submitted on : Tuesday, February 28, 2017 - 11:09:11 AM
Last modification on : Friday, May 29, 2020 - 6:28:19 AM

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Azza Mensi, Yvan Choiset, Hanitra Rabesona, Thomas Haertlé, Patrick Borel, et al.. Interactions of β-Lactoglobulin Variants A and B with Vitamin A. Competitive Binding of Retinoids and Carotenoids. Journal of Agricultural and Food Chemistry, American Chemical Society, 2013, 61 (17), pp.4114 - 4119. ⟨10.1021/jf400711d⟩. ⟨inserm-01478545⟩

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