Hydroxyapatite Growth Inhibition Effect of Pellicle Statherin Peptides

• Published in: Journal of dental research Vol. 94; no. 8; pp. 1106 - 1112
• Main Authors: Xiao, Y., Karttunen, M., Jalkanen, J., Mussi, M.C.M., Liao, Y., Grohe, B., Lagugné-Labarthet, F., Siqueira, W.L.
• Format: Journal Article
• Language: English
• Published: Los Angeles, CA SAGE Publications 01.08.2015; SAGE PUBLICATIONS, INC
• Subjects: Adsorption; Calcium phosphates; Colorimetry; Crystallization; Dental calculus; Dental caries; Dental enamel; Dental Enamel Proteins - analysis; Dental Enamel Proteins - chemistry; Dental Pellicle - chemistry; Dentistry; Durapatite - chemistry; Enamel; Hydroxyapatite; Hypotheses; Molecular weight; Pellicle; Peptides; Periodontal diseases; Phosphorylation; Proteins; Salivary Proteins and Peptides - analysis; Salivary Proteins and Peptides - chemistry; Spectrum Analysis, Raman; Synthetic peptides; saliva; dental caries; dental calculus; molecular dynamics; proteins; enamel pellicle
• ISSN: 0022-0345; 1544-0591
• DOI: 10.1177/0022034515586769

In our recent studies, we have shown that in vivo–acquired enamel pellicle is a sophisticated biological structure containing a significant portion of naturally occurring salivary peptides. From a functional aspect, the identification of peptides in the acquired enamel pellicle is of interest because many salivary proteins exhibit functional domains that maintain the activities of the native protein. Among the in vivo–acquired enamel pellicle peptides that have been newly identified, 5 peptides are derived from statherin. Here, we assessed the ability of these statherin pellicle peptides to inhibit hydroxyapatite crystal growth. In addition, atomistic molecular dynamics (MD) simulations were performed to better understand the underlying physical mechanisms of hydroxyapatite growth inhibition. A microplate colorimetric assay was used to quantify hydroxyapatite growth. Statherin protein, 5 statherin-derived peptides, and a peptide lacking phosphate at residues 2 and 3 were analyzed. Statherin peptide phosphorylated on residues 2 and 3 indicated a significant inhibitory effect when compared with the 5 other peptides (P < 0.05). MD simulations showed a strong affinity and fast adsorption to hydroxyapatite for phosphopeptides, whereas unphosphorylated peptides interacted weakly with the hydroxyapatite. Our data suggest that the presence of a covalently linked phosphate group (at residues 2 and 3) in statherin peptides modulates the effect of hydroxyapatite growth inhibition. This study provides a mechanism to account for the composition and function of acquired enamel pellicle statherin peptides that will contribute as a base for the development of biologically stable and functional synthetic peptides for therapeutic use against dental caries and/or periodontal disease.