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Journal of Dairy Science Vol. 81 No. 12 3139-3148
© 1998 by American Dairy Science Association ®
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Conformational Studies of a Synthetic Peptide from the Putative Lipid-binding Domain of Bovine Milk Component PP3

S. Campagna 1, B. Vitoux 2, G. Humbert 1, J. M. Girardet 1, G. Linden 1, T. Haertle 3, and J. L. Gaillard 1

1 Laboratoire des BioSciences de l'Aliment, Unité associée à l'Institut National de la Recherche Agronomique, Université H. Poincaré-Nancy 1, 54506 Vandoeuvre-lès-Nancy, France
2 Laboratoire de Cristallographie et Modélisation des Matériaux Minéraux et Biologiques, Unité Propre de Recherche de l'Enseignement Supérieur Associée au Centre National de la Recherche Scientifique 7036, Université H. Poincaré-Nancy 1, 54506 Vandoeuvre-lès-Nancy, France
3 Laboratoire d'Etude des Interactions des Molécules Alimentaires, Institut National de la Recherche Agronomique, rue de la Géraudière, BP 71627, 44316 Nantes, France

In bovine milk, a glycosylated phosphoprotein, component PP3, is known for its remarkable emulsifying properties and its capability to inhibit lipolytic activities. The determination of its primary structure is not sufficient to explain these properties. Secondary structure predictions of component PP3 and of its homologous proteins were achieved using a combination of multiple predictive methods. Based on this study, the f 119–135 region of component PP3 was proposed to be likely to adopt an amphipathic helical conformation, which is a lipid-binding motif. The conformation of the synthetic peptide corresponding to the C-terminal f 119–135 part of bovine component PP3 was analyzed by circular dichroism experiments using various media. The circular dichroism data indicated that the peptide was able to form an amphipathic alpha-helix structure in trifluoroethanol as well as in the presence of sodium dodecyl sulfate or acidic and neutral lipids, but not in water. Moreover, the conformation of this peptide is solvent dependent because it was found to adopt a ß-sheet structure for low concentrations of sodium dodecyl sulfate or a low molar ratio of acidic lipid to peptide. Tensiometric measurements showed that the amphipathic C-terminal region of component PP3 is highly tensioactive and, thus, must be responsible for the particular behavior of the protein in emulsions.

Key Words: component PP3 • amphipathic helix • secondary structure prediction • circular dichroism

Submitted on February 11, 1998
Accepted on June 29, 1998




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S. Campagna, A.-G. Mathot, Y. Fleury, J.-M. Girardet, and J.-L. Gaillard
Antibacterial Activity of Lactophoricin, a Synthetic 23-Residues Peptide Derived from the Sequence of Bovine Milk Component-3 of Proteose Peptone
J Dairy Sci, June 1, 2004; 87(6): 1621 - 1626.
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