Casein Phosphopeptide-Amorphous Calcium Phosphate Nanocomplexes: A Structural Model

Tryptic digestion of the calcium-sensitive caseins yields casein phosphopeptides (CPP) that contain clusters of phosphorylated seryl residues. The CPP stabilize calcium and phosphate ions through the formation of complexes. The calcium phosphate in these complexes is biologically available for intestinal absorption and remineralization of subsurface lesions in tooth enamel. We have studied the structure of the complexes formed by the CPP with calcium phosphate using a variety of nuclear magnetic resonance (NMR) techniques. Translational diffusion measurements indicated that the beta-CN(1-25)-ACP nanocomplex has a hydrodynamic radius of 1.526 +/- 0.044 nm at pH 6.0, which increases to 1.923 +/- 0.082 nm at pH 9.0. H-1 NMR spectra were well resolved, and (3)JH(N)-H-alpha measurements ranged from a low of 5.5 Hz to a high of 8.1 Hz. Total correlation spectroscopy and nuclear Overhauser effect spectroscopy spectra were acquired and sequentially assigned. Experiments described in this paper have allowed the development of a structural model of the beta-CN(1-25) amorphous calcium phosphate nanocomplex.