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. 2016 Jun 9;17(6):915.
doi: 10.3390/ijms17060915.

The Interactions of CPP-ACP with Saliva

Noorjahan Laila Huq  1 , Helen Myroforidis  2 , Keith J Cross  3 , David P Stanton  4 , Paul D Veith  5 , Brent R Ward  6 , Eric C Reynolds  7
Affiliations

The Interactions of CPP-ACP with Saliva

Noorjahan Laila Huq et al. Int J Mol Sci. .

Abstract

The repair of early dental caries lesions has been demonstrated by the application of the remineralisation technology based on casein phosphopeptide-stabilised amorphous calcium phosphate complexes (CPP-ACP). These complexes consist of an amorphous calcium phosphate mineral phase stabilised and encapsulated by the self-assembly of milk-derived phosphopeptides. During topical application of CPP-ACP complexes in the oral cavity, the CPP encounters the enamel pellicle consisting of salivary proteins and peptides. However the interactions of the CPP with the enamel salivary pellicle are not known. The studies presented here reveal that the predominant peptides of CPP-ACP complexes do interact with specific salivary proteins and peptides of the enamel pellicle, and provide a mechanism by which the CPP-ACP complexes are localised at the tooth surface to promote remineralisation.

Keywords: casein phosphopeptide; enamel; pellicle; saliva.

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Figures

Figure 1
Figure 1
The sequences of the two major casein tryptic phosphopeptides with the calcium phosphate binding-motif underlined are depicted using the three-letter code.
Figure 2
Figure 2
SDS-PAGE profile of salivary proteins derived from whole saliva (WS) bound to casein phosphopeptides (CPP)-coated or uncoated HA. Lane 1: Salivary proteins not bound to β-CN (1–25). Lane 2: Salivary proteins bound to β-CN (1–25). Lane 3: WS. Lane 4: Salivary proteins bound to αS1-CN (59–79). Lane 5: Salivary proteins not bound to αS1-CN (59–79). Lane 6: WS diluted 1 in 20. Lane 7: WS. Lane 8: Salivary proteins bound to uncoated HA control. Lane 9: Salivary proteins not bound to uncoated HA. Lane 10: Prestained markers.
Figure 3
Figure 3
Mass and pI distribution of salivary proteins and peptides of human acquired enamel pellicle that bind to CPP (αS1-CN (59–79), β-CN (1–25)).
Figure 4
Figure 4
ELISA of αS1-CN (59–79) binding to whole saliva (blue squares) and parotid saliva (red circles) and β-CN (1–25) binding to whole saliva (white diamonds).
Figure 5
Figure 5
ELISA of αS1-CN (59–79) (triangles) and β-CN (1–25) (squares) binding to (A) Histatin 1; (B) Statherin; (C) Amylase; (D) Albumin.
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References

    1. Loesche W. Role of Streptococcus mutans in human dental decay. Microbiol. Rev. 1986;50:353–380. - PMC - PubMed
    1. Featherstone J.D.B. Dental caries: A dynamic disease process. Aust. Dent. J. 2008;53:286–291. doi: 10.1111/j.1834-7819.2008.00064.x. - DOI - PubMed
    1. Bradshaw D.J., Lynch R.J. Diet and the microbial aetiology of dental caries: New paradigms. Int. Dent. J. 2013;63:64–72. doi: 10.1111/idj.12082. - DOI - PMC - PubMed
    1. Merritt J., Qi F., Shi W. Milk helps build strong teeth and promotes oral health. J. Calif. Dent. Assoc. 2006;34:361–366. - PubMed
    1. Aimutis W.R. Bioactive properties of milk proteins with particular focus on anticariogenesis. J. Nutr. 2004;134:989S–995S. - PubMed

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