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


IATE, Université de Montpellier, CIRAD, INRA, Montpellier SupAgro, Montpellier, France. Electronic address: [Email]


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).


Binding parameters,Curcumin,Curcumin (PubChem CID 969516),Fluorescence quenching,Surface plasmon resonance,Vitamin D3,Vitamin D3 (PubChem CID 5280795),β-Casein,

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