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Topography of the casein micelle surface by surface plasmon resonance (SPR) using a selection of specific monoclonal antibodies.

Authors
  • Dupont, Didier
  • Johansson, Annette
  • Marchin, Stephane
  • Rolet-Repecaud, Odile
  • Marchesseau, Sylvie
  • Leonil, Joelle
Type
Published Article
Journal
Journal of Agricultural and Food Chemistry
Publisher
American Chemical Society
Publication Date
Aug 10, 2011
Volume
59
Issue
15
Pages
8375–8384
Identifiers
DOI: 10.1021/jf2024038
PMID: 21740045
Source
Medline
License
Unknown

Abstract

Several theoretical models of the casein micelle structure have been proposed in the past, but the exact organization of the four individual caseins (α(s1), α(s2), β, and κ) 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 α(s1)-, α(s2)-, β-, and κ-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 κ-casein was highly accessible and located at the periphery of the structure. When casein micelles were submitted to proteolysis, the C-terminal extremity of κ-casein was rapidly hydrolyzed. Disintegration of the micellar structure resulted in an increased access for antibodies to hydrophobic areas of α(s1)- and α(s2)-casein.

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