CHARACTERIZATION OF LOW-MOLECULAR-WEIGHT PEPTIDES IN HUMAN PAROTID-SALIVA

The low-molecular-weight components of human saliva remain poorly char acterized. Therefore, low-molecular-weight peptides (Mr < 3000) have b een purified from human parotid saliva and characterized with respect to their amino acid sequence. From the sequences obtained, it is likel y that these peptides are derived from proteolysis of the hydroxyapati te-interactive human salivary proteins, histatins, proline-rich protei ns, and statherins. Since human parotid saliva is an amicrobial fluid, much of the low-molecular-weight peptide fraction of this secretion a ppears to be derived from the proteolytic processing of the larger pro teins. Because of their small size, these peptides are likely to be in exchange with dental plaque fluid and may therefore help modulate eve nts such as demineralization/remineralization, microbial attachment, a nd dental plaque metabolism at the tooth-saliva interface.