Publication: Phosphorylation of osteopontin peptides mediates adsorption to and incorporation into calcium oxalate crystals
All || By Area || By Year| Title | Phosphorylation of osteopontin peptides mediates adsorption to and incorporation into calcium oxalate crystals | Authors/Editors* | J. O'Young, S. Chirico, N. al-Tarhuni, B. Grohe, M. Karttunen, H.A. Goldberg and G.K. Hunter |
|---|---|
| Where published* | Cells Tissues Organs |
| How published* | Journal |
| Year* | 2009 |
| Volume | 189 |
| Number | |
| Pages | 51-55 |
| Publisher | Karger |
| Keywords | |
| Link | |
| Abstract |
Phosphorylated peptides of osteopontin (OPN) have been shown to inhibit the growth of the {100} face of calcium oxalate monohydrate (COM). The inhibitory potency has been shown to be dependent on the phosphate content of the peptide. The purpose of this study is to better understand the means by which phosphate groups promote crystal growth inhibition by OPN peptides. Peptides of rat bone OPN 220â235 have been synthesized with zero(P0), 1 (P1) or 3 (P3) phosphate modifications. COM crystals were grown in the presence of 0.1â10 ug of P0, P1 or P3. P0 incorporation into COM crystals was evident at 10 ug/ml of peptide, whereas the phosphorylated peptides P1 and P3 were incorporated at all tested concentrations. At 5 ug/ml of P3, COM crystals exhibited a âdumbbellâ morphology. To study the peptide-mineral interaction, surface frequencyplots were constructed from molecular dynamics simulations of OPN peptide adsorption. Carboxylate and phosphate groups were found to adsorb in specific orientations to the COM {100} surface. In conclusion, it appears that the phosphate groups on OPN peptides are capable of interacting with the COM {100} surface. This interaction appears to increase the adsorption energy of the peptide to the surface, thus enhancing its inhibitory potency. |
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