This title appears in the Scientific Report : 2015 

Hydroxyapatite Growth Inhibition Effect of Pellicle Statherin Peptides
Xiao, Y.
Karttunen, M. / Jalkanen, J. / Mussi, M. C. M. / Liao, Y. / Grohe, B. / Lagugne-Labarthet, F. / Siqueira, W. L. (Corresponding author)
Jülich Supercomputing Center; JSC
Journal of dental research, 94 (2015) 8, S. 1106 - 1112
Thousand Oaks, Calif. Sage 2015
26116492
10.1177/0022034515586769
Journal Article
Computational Science and Mathematical Methods
Please use the identifier: http://dx.doi.org/10.1177/0022034515586769 in citations.
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.