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Added by mollevi
Last modified by alainmange
Group name PlateformePP2I
Item Type Journal Article
Title Binding analysis between monomeric ?-casein and hydrophobic bioactive compounds investigated by surface plasmon resonance and fluorescence spectroscopy
Creator Bahri et al.
Author Asma Bahri
Author Corinne Henriquet
Author Martine Pugnière
Author Sylvie Marchesseau
Author Dominique Chevalier-Lucia
Abstract ?-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 ?-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-?-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 ?-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 ?-casein (KA?=?23.5?±?1.9?×?104?M-1) than vitamin D3 (KA?=?5.8?±?1.1?×?104?M-1).
Publication Food Chemistry
Volume 286
Pages 289-296
Date Jul 15, 2019
Journal Abbr Food Chem
Language eng
DOI 10.1016/j.foodchem.2019.01.176
ISSN 1873-7072
Library Catalog PubMed
Extra PMID: 30827608
Tags ?-Casein, Animals, author, Binding parameters, Caseins, Cattle, Cholecalciferol, Curcumin, Curcumin (PubChem CID 969516), Fluorescence quenching, Hydrophobic and Hydrophilic Interactions, Micelles, Milk, original, pp2i, Protein Binding, Spectrometry, Fluorescence, Surface Plasmon Resonance, Vitamin D3, Vitamin D3 (PubChem CID 5280795)
Date Added 2019/06/04 - 17:17:14
Date Modified 2020/01/14 - 10:24:59


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