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Binding analysis between monomeric β-casein and hydrophobic bioactive compounds investigated by surface plasmon resonance and fluorescence spectroscopy

Abstract : β-Casein, a phosphoprotein representing 37% of the bovine milk caseins, has specific features promoting its application as a nanocarrier for hydrophobic bioactives. In this study, the interactions of β-casein with curcumin and vitamin D3 under the same physico-chemical conditions were investigated. The interaction kinetics have been studied by surface plasmon resonance (SPR) and fluorescence spectroscopy. The KD value for curcumin-β-casein interaction has been successfully evaluated (4.1 ± 0.7 × 10−4 M) using SPR by fitting data to a 1:1 Langmuir interaction model. Conversely, the SPR responses obtained for vitamin D3 show that the interactions between this hydrophobic compound and the β-casein immobilized on the sensor chip were below the sensitivity of the SPR apparatus. Moreover, the fluorescence quenching data show that curcumin has higher affinity to β-casein (KA = 23.5 ± 1.9 × 104 M−1) than vitamin D3 (KA = 5.8 ± 1.1 × 104 M−1).
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Asma Bahri, Corinne Henriquet, Martine Pugnière, Sylvie Marchesseau, Dominique Chevalier-Lucia. Binding analysis between monomeric β-casein and hydrophobic bioactive compounds investigated by surface plasmon resonance and fluorescence spectroscopy. Food Chemistry, Elsevier, 2019, 286, pp.289-296. ⟨10.1016/j.foodchem.2019.01.176⟩. ⟨hal-02048380⟩

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