Interactions of matrix proteins from mineralized tissues with octacalcium phosphate

H. Furedi-Milhofer*, J. Moradian-Oldak, S. Weiner, A. Veis, K. P. Mintz, L. Addadf

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

87 Scopus citations


Acidic matrix macromolecules, present in many mineralized tissues, including those of vertebrates, are thought to be involved in controlling crystal formation. Little, however, is known about their in vivo functions, particularly in relation to calcium-phosphate-containing crystals. The manner in which a variety of synthetic and natural acidic macromolecules interact in vitro with crystals of octacalcium phosphate (OCP) has been studied. Interactions were assessed by examining changes in morphology of the crystals resulting from preferential interaction of the additive with some crystal faces and not others. Macromolecules rich in acidic amino acids, with or without polysaccharides, such as polyaspartate and mollusk shell proteins respectively, were shown to interact preferentially with rows of Ca ions exposed on the hydrated plate surface of OCP crystals. In contrast, the phosphorylated proteins, phosphophoryn and phosvitin, interacted specifically with the apatite-like motifs on the OCP side faces. BSP did not interact specifically with OCP, under the experimental conditions used. The observation that these classes of acidic macromolecules recognize different crystal faces should be taken into account when evaluating functions of acidic matrix macromolecules in mineralized tissues.

Original languageEnglish (US)
Pages (from-to)251-264
Number of pages14
JournalConnective tissue research
Issue number4
StatePublished - 1994


  • Biomineralization
  • Hydroxyapatite
  • Octacalcium phosphate
  • Phosphophoryn

ASJC Scopus subject areas

  • Rheumatology
  • Biochemistry
  • Orthopedics and Sports Medicine
  • Molecular Biology
  • Cell Biology


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