Journal article
How Does Bone Sialoprotein Promote the Nucleation of Hydroxyapatite? A Molecular Dynamics Study Using Model Peptides of Different Conformations
Langmuir, v 26(12), pp 9848-9859
15 Jun 2010
PMID: 20438109
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Bone sialoprotein (BSP) is a highly phosphorylated, acidic, noncollagenous protein in bone matrix. Although BSI has been proposed to be a nucleator of hydroxyapatite (Ca-5(PO4)(3)OH), the major mineral component of bone, no detailed mechanism for the nucleation process has been elucidated at the atomic level to date. In the present work, using a peptide model, we apply molecular dynamics (MD) simulations to study the conformational effect of a proposed nucleating motif of BSP (a phosphorylated, acidic, 10 amino-acid residue sequence) on controlling the distributions of Ca2+ and inorganic phosphate (Pi) ions in solution, and specifically, we explore whether a nucleating template for orientated hydroxyapatite could be formed in different peptide conformations. Both the alpha-helical conformation and the random coil structure have been studied, and inorganic solutions without the peptide are simulated as reference. Ca2+ distributions around the peptide surface and interactions between Ca2+ and Pi in the presence of the peptide are examined in detail. From the MD simulations, although in some cases for the a-helical conformation, we observe that a Ca2+ equilateral triangle forms around the surface of peptide, which matches the distribution of Ca2+ ions on the (001) face of the hydroxyapatite crystal, we do not consistently find a stable nucleating template formation in general for either the helical conformation or the random coil structure. Therefore, independent of conformations, the BSP nucleating motif is more likely to help nucleate an amorphous calcium phosphate cluster, which ultimately converts to crystalline hydroxyapatite.
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Details
- Title
- How Does Bone Sialoprotein Promote the Nucleation of Hydroxyapatite? A Molecular Dynamics Study Using Model Peptides of Different Conformations
- Creators
- Yang Yang - Drexel University, ChemistryQiang Cui - University of Wisconsin–MadisonNita Sahai - University of Akron
- Publication Details
- Langmuir, v 26(12), pp 9848-9859
- Publisher
- Amer Chemical Soc
- Number of pages
- 12
- Grant note
- Department of Geoscience Weeks Endowment National Center for Supercomputing Applications (NCSA) 41777-AC2 / American Chemical Society Petroleum Research Fund; American Chemical Society NASA Astrobiology Institute EAR 0346689 / National Scientific Foundation CAREER Award
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Chemistry
- Web of Science ID
- WOS:000278427600093
- Scopus ID
- 2-s2.0-77956085282
- Other Identifier
- 991021874714604721
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Data related to this publication, from InCites Benchmarking & Analytics tool:
- Web of Science research areas
- Chemistry, Multidisciplinary
- Chemistry, Physical
- Materials Science, Multidisciplinary