Interactions of a human salivary proline-rich glycoprotein nonapeptide functional domain with model surfaces

Abstract

The homeostasis of the tooth's hydroxyapatite-like surface is primarily maintained by a proteinaceous film called the acquired enamel pellicle (AEP). Human saliva contains a family of proline-rich proteins (PRPs) which are among the first biomolecules to adsorb to the tooth's surface, and consequently are deemed essential to AEP formation and function. One particular member of the PRPs, the proline-rich glycoprotein (PRG), has several areas of conserved sequence. One of these regions, G(1)-P(2)-P(3)-P(4)-H(5)-P(6)-G(7)-K(8)-P(9), or PRG9, occurs twice and has several proline residues occurring in different types of physico-chemical environments. An investigation into the static and dynamic adsorption processes of this peptide onto model surfaces (i.e. non-siliconized and siliconized germanium plates) was accomplished in this study. PRG9 was found to adsorb tightly to the non-siliconized germanium plates at near-monolayer thicknesses in both the static and the dynamic flow experiments. However, the peptide...