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Vol. 189, No. 1-4, 2009
Issue release date: December 2008
Section title: Paper
Cells Tissues Organs 2009;189:51–55
(DOI:10.1159/000151724)

Phosphorylation of Osteopontin Peptides Mediates Adsorption to and Incorporation into Calcium Oxalate Crystals

O’Young J.a · Chirico S.a · Al Tarhuni N.a · Grohe B.a · Karttunen M.b · Goldberg H.A.a · Hunter G.K.a
aSchool of Dentistry and CIHR Group in Skeletal Development and Remodeling and bDepartment of Applied Mathematics, University of Western Ontario, London, Ont., Canada

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Article / Publication Details

First-Page Preview
Abstract of Paper

Published online: 8/26/2008
Issue release date: December 2008

Number of Print Pages: 5
Number of Figures: 3
Number of Tables: 1

ISSN: 1422-6405 (Print)
eISSN: 1422-6421 (Online)

For additional information: http://www.karger.com/CTO

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 220–235 peptides have been synthesized with zero (P0), 1 (P1) or 3 (P3) phosphate modifications. COM crystals were grown in the presence of 0.1–10 μg of P0, P1 or P3. P0 incorporation into COM crystals was evident at 10 μg/ml of peptide, whereas the phosphorylated peptides P1 and P3 were incorporated at all tested concentrations. At 5 μg/ml of P3, COM crystals exhibited a ‘dumbbell’ morphology. To study the peptide-mineral interaction, surface frequency plots 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.


  

Author Contacts

Dr. Graeme K. Hunter
CIHR Group in Skeletal Development and Remodeling
Schulich School of Medicine and Dentistry, University of Western Ontario
London, ON N6A 5C1 (Canada)
Tel. +1 519 661 2185, Fax +1 519 850 2459, E-Mail graeme.hunter@schulich.uwo.ca

  

Article Information

Published online: August 26, 2008
Number of Print Pages : 5
Number of Figures : 3, Number of Tables : 1, Number of References : 13

  

Publication Details

Cells Tissues Organs (in vivo, in vitro)

Vol. 189, No. 1-4, Year 2009 (Cover Date: December 2008)

Journal Editor: Denker H.-W. (Essen), English A.W. (Atlanta, Ga.)
ISSN: 1422-6405 (Print), eISSN: 1422-6421 (Online)

For additional information: http://www.karger.com/CTO


Article / Publication Details

First-Page Preview
Abstract of Paper

Published online: 8/26/2008
Issue release date: December 2008

Number of Print Pages: 5
Number of Figures: 3
Number of Tables: 1

ISSN: 1422-6405 (Print)
eISSN: 1422-6421 (Online)

For additional information: http://www.karger.com/CTO


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