Mineralisation of soft and hard tissues and the stability of biofluids

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  • Carl Holt, Institute of Molecular, Cell and Systems Biology, University of Glasgow, Glasgow G12 8QQ, UK. Electronic address: carl.holt@glasgow.ac.uk., Storbritannien
  • Samuel Lenton, EPSAM, Keele University, Staffordshire ST5 5BG, UK; Institut Laue-Langevin, 6 Rue Jules Horowitz, 38042 Grenoble, France. Electronic address: lenton@ill.fr., Frankrig
  • Tommy Nylander, Lund University, Sverige
  • Esben Skipper Sørensen
  • Susana C M Teixeira, EPSAM, Keele University, Staffordshire ST5 5BG, UK; Institut Laue-Langevin, 6 Rue Jules Horowitz, 38042 Grenoble, France. Electronic address: teixeira@ill.fr., Frankrig
Evidence is provided from studies on natural and artificial biofluids that the sequestration of amorphous calcium phosphate by peptides or proteins to form nanocluster complexes is of general importance in the control of physiological calcification. A naturally occurring mixture of osteopontin peptides was shown, by light and neutron scattering, to form calcium phosphate nanoclusters with a core-shell structure. In blood serum and stimulated saliva, an invariant calcium phosphate ion activity product was found which corresponds closely in form and magnitude to the ion activity product observed in solutions of these osteopontin nanoclusters. This suggests that types of nanocluster complexes are present in these biofluids as well as in milk. Precipitation of amorphous calcium phosphate from artificial blood serum, urine and saliva was determined as a function of pH and the concentration of osteopontin or casein phosphopeptides. The position of the boundary between stability and precipitation was found to agree quantitatively with the theory of nanocluster formation. Artificial biofluids were prepared that closely matched their natural counterparts in calcium and phosphate concentrations, pH, saturation, ionic strength and osmolality. Such fluids, stabilised by a low concentration of sequestering phosphopeptides, were found to be highly stable and may have a number of beneficial applications in medicine.
OriginalsprogEngelsk
TidsskriftJournal of Structural Biology
Vol/bind185
Nummer3
Sider (fra-til)383-396
Antal sider14
ISSN1047-8477
DOI
StatusUdgivet - mar. 2014

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