Résumé
Several theoretical models of the casein micelle structure have been proposed in the past, but the exact organization of the four individual caseins (alpha(s1), alpha(s2), beta, and kappa) within this supramolecular structure remains unknown. The present study aims at determining the topography of the casein micelle surface by following the interaction between 44 monoclonal antibodies specific for different epitopes of alpha(s1)-, alpha(s2)-, beta-, and kappa-casein and the casein micelle in real time and no labeling using a surface plasmon resonance (SPR)-based biosensor. Although the four individual caseins were found to be accessible for antibody binding, data confirmed that the C-terminal extremity of kappa-casein was highly accessible and located at the periphery of the structure. When casein micelles were submitted to proteolysis, the C-terminal extremity of kappa-casein was rapidly hydrolyzed. Disintegration of the micellar structure resulted in an increased access for antibodies to hydrophobic areas of alpha(s1)- and alpha(s2)-casein.