CPP-ACP IS CALLED AS RECALDENT
Recaldent was developed by Professor Eric Reynolds in the School of Dental Science at the University of Melbourne.
The casein phosphopeptides can be easily prepared from a tryptic digest of caseinate by selective precipitation with Ca2+ in the presence of ethanol (Reynolds, 1991). This produces a casein phosphopeptide (CPP) fraction rich in the phosphopeptides aLS-CN(59-79) and PCN(l /2-25)
Although the calcium, phosphate and fluoride ions are stabilized by the CPP from promoting dental calculus, during acidogenic challenges, nano-complexes release calcium and phosphate ions via a pH or concentration gradient mechanism to maintain a supersaturated environment with respect to hydroxyapatite
CPP-ACP was incorporated into supragingival dental plaque by binding onto the surfaces of bacterial cells, as well as to components of the intercellular plaque matrix, and significantly increased the plaque levels of calcium (Ca) and inorganic phosphate (Pi).
The bacterial cell contains both hydrophilic and hydrophobic molecules on its surface (Rose et al., 1997). The CPP molecules also contain hydrophilic and hydrophobic regions, and it is possible that binding to the bacterial cell surface is mediated by Ca2+ cross-linking of the negative charges on the peptide and the cell surface molecules (e.g,phosphoryl and carboxylate groups) as well as by hydrophobic and hydrogen-bond-mediated interactions.
CPP-ACP would compete with calcium for plaque Ca binding sites. This will reduce the amount of calcium bridging between the pellicle and adhering cells and between cells themselves
As the pH decreases CPP-ACP residues become protonated thereby releasing calcium together with its associated anions. Hence, CPP can act as a reservoir for calcium, phosphate and fluoride ions.
remineralized enamel indicated that the mineral deposited was hydroxyapatite with a higher Ca:P ratio than normal apatite. remineralized apatite was more resistant to acid challenge than the normal calciumdeficient carbonated tooth enamel.
CPP act as a delivery vehicle to co-localize bioavailable calcium,fluoride and phosphate ions at the tooth surface.
casein proteins are capable of decreasing the rate of precipitation of calcium phosphate from a moderately supersaturated solution at concentrations, suggesting that the very rapid interaction of the phosphoprotein with calcium phosphate nuclei in such solutions is aided by the open and generally flexible conformation of casein produce nanometre-sized particles of calcium phosphate stabilized by a casein phosphopeptide.
IT IS COMMERCIALLY AVAILABLE AS TOOTH MOUSE
The sugar-free gums (control and CPP-ACP containing gums) were chewed for either 20- minute periods, four times a day or for 5-minute periods, seven times a day.
GIC CONTAINGING CPP-ACP
The CPP-ACP nanoparticles may have been physically encapsulated into the set GIC, as has been found with
unreacted glass particles (Matsuya et al., 1984), and therefore released as the acid eroded the cement in the acidic buffer.
The acid-catalyzed release of the CPP-ACP nanoparticles from the GIC is consistent with the protection of the adjacent dentin observed during acid challenge
The CPP-ACP in the GIC may have also directly increased microtensile bond strength by the incorporation of the CPP-ACP nanoparticles into the crosslinked matrix of the GIC.
reference
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