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J. Biol. Chem., Vol. 275, Issue 21, 16213-16218, May 26, 2000
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From the Extracellular matrix proteins play key roles in
controlling the activities of osteoblasts and osteoclasts in bone
remodeling. These bone-specific extracellular matrix proteins contain
amino acid sequences that mediate cell adhesion, and many of the
bone-specific matrix proteins also contain acidic domains that interact
with the mineral surface and may orient the signaling domains. Here we
report a fusion peptide design that is based on this natural approach
for the display of signaling peptide sequences at biomineral surfaces.
Salivary statherin contains a 15-amino acid hydroxyapatite binding
domain (N15) that is loosely helical in solution. To test whether N15
can serve to orient active peptide sequences on hydroxyapatite, the RGD
and flanking residues from osteopontin were fused to the C terminus.
The fusion peptides bound tightly to hydroxyapatite, and the N15-PGRGDS
peptide mediated the dose-dependent adhesion of
Mo
Chimeric Peptides of Statherin and Osteopontin That Bind
Hydroxyapatite and Mediate Cell Adhesion*
,,,, and¶
Department of Bioengineering and
§ Department of Chemistry, University of Washington,
Seattle, Washington 98195
v melanoma cells when immobilized on the
hydroxyapatite surface. Experiments with an integrin-sorted
Mov subpopulation demonstrated that the
v
3 integrin was the primary receptor
target for the fusion peptide. Solid state NMR experiments showed that the RGD portion of the hydrated fusion peptide is highly dynamic on the
hydroxyapatite surface. This fusion peptide framework may thus provide
a straightforward design for immobilizing bioactive sequences on
hydroxyapatite for biomaterials, tissue engineering, and vaccine applications.
*
This work was supported by National Institutes of Health
NIDR Grant DE 12554-01, National Science Foundation University of Washington Engineered Biomaterials Engineering Research Center Grant
EEC-9529161, a Whitaker Foundation graduate fellowship (to M. G.),
and the Office of Science, Office of Basic Energy Sciences, Department
of Energy, through an Associated Western Universities graduate
fellowship (to W. J. S).The costs of publication of this article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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