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ItemMolecular Interactions of Peptide Encapsulated Calcium Phosphate Delivery Vehicle at Enamel SurfacesHuq, NL ; Cross, KJ ; Myroforidis, H ; Stanton, DP ; Chen, YY ; Ward, BR ; Reynolds, EC ; Nagasawa, H ; Kogure, T ; Endo, K (Springer, 2018-12-31)Phosphorylated peptides derived from milk caseins, known as casein phosphopeptides (CPP) self-assemble and encapsulate the calcium and phosphate mineral in the form of amorphous calcium phosphate (ACP) thus forming CPP-ACP nanocomplexes that are non-toxic and bio-compatible. The biomedical application is the repair of tooth surfaces (enamel) at early stages of tooth decay. These nanocomplexes release calcium and phosphate ions to rebuild demineralised HA crystals in enamel subsurface lesions. The topical application of CPP-ACP at the tooth surface initiates a series of interactions at the enamel mineral hydroxyapatite surface, and at the enamel salivary pellicle that are not well understood. In this study, we have shown that the β-casein (1-25) peptide binds reversibly to Ca2+, Mg2+, Mn2+, La2+, Ni2+, and Cd2+ metal ions. In contrast, binding to Sn2+, Fe2+, and Fe3+ ions, resulted in ion-induced aggregation. The casein peptides as well as the mineral ions dissociate from the CPP-ACP complexes to adsorb to both the un-coated and saliva-coated mineral surface with the mineralisation increasing monotonically with increasing pH. Furthermore, SEM of the CPP-ACP revealed images of spherical particles surrounded by ACP mineral. In conclusion, the enamel remineralisation process involves an array of interactions between the peptide and mineral ions of the CPP-ACP delivery vehicle and the tooth enamel mineral with its salivary pellicle.