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Calcium Mineral-Peptide Interactions

Published online by Cambridge University Press:  21 February 2011

A. P. Wheeler  and
C. Steven Sikes
A. P. Wheeler
Affiliation:
Department of Biological Sciences, Clemson University, Clemson, SC 29634
C. Steven Sikes
Affiliation:
Mineralization Center, University of South Alabama, Mobile, AL 36688
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Abstract

Peptides have been synthesized by solid phase methods with structures which are in part based on experimentally-determined features of a major class of organic matrix phosphoproteins isolated from the calcium carbonate shell of the oyster. The matrix structures mimicked in the synthetic peptides included runs of aspartic acid (Asp), which were contrasted with peptides having other deployments of Asp with serine (Ser) and glycine (Gly). In addition, peptide-Ser was phosphorylated (PSer) and the hydrophobic carboxyterminus of natural matrix was mimicked using polyalanine tails. The interaction of the various peptides with CaCO3 as well as calcium phosphates was determined using a variety of crystallization assays and studies of adsorption of radio-labelled peptides to crystal surfaces.

In general, peptides that include runs of Asp regulate crystal nucleation and growth more effectively than those which contain (Asp-X)n or (Asp-X-Y)n sequences with X and Y being either Gly or Ser. Further, CaCO3 crystals have a much higher binding capacity for polyAsp than for peptides with other deployments of Asp. Phosphorylation increases the regulatory activity and the crystal capacities of Asp/Ser - containing peptides. PolyAsp peptides having terminal PSer's are especially effective as regulators of CaCO3 nucleation and the conversion of amorphous calcium phosphate to apatite. The activity of Asp15 molecules in CaCO3 nucleation assays is markedly increased by the addition of polyalanine tails.

Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 174: Symposium R – Materials Synthesis Utilizing Biological Processes , 1989 , 45
Copyright
Copyright © Materials Research Society 1990

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References

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