Phosphopeptides derived from human salivary acidic proline-rich proteins. Biological activities and concentration in saliva

Abstract

Human saliva contains a large number of phosphopeptides derived by cleavage of acidic proline-rich proteins (APRPs). These peptides were purified by column chromatography and they constituted 0.5% of APRPs in parotid saliva, but 11% of APRPs in saliva expectorated from the mouth (whole saliva), indicating that there is considerable cleavage of APRPs after secretion from the gland. Similarly to APRP, the phosphopeptides bind Ca2+, but they accounted for only 4% of protein-bound Ca2+ in whole saliva. APRPs as well as the phosphopeptides inhibited formation of hydroxyapatite, but, whereas 19-20 micrograms of APRP was needed for 50% inhibition, only 0.7-3.3 micrograms of purified peptides was needed for the same degree of activity, and the phosphopeptides accounted for 18% of total inhibitory activity in whole saliva. All phosphopeptides adsorbed on hydroxyapatite in vitro, and adsorption of phosphopeptides on tooth surfaces in vivo could also be demonstrated, indicating that they would be able to inhibit unwanted mineral formation on the tooth surface in vivo. Degradation of APRPs after secretion therefore does not lead to a loss of their biological activities.