HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 275, Issue 21, 16213-16218, May 26, 2000

This Article Full Text Full Text (PDF) All Versions of this Article: 275/21/16213    most recent M001773200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Gilbert, M. Articles by Stayton, P. S. Search for Related Content PubMed PubMed Citation Articles by Gilbert, M. Articles by Stayton, P. S. Social Bookmarking                      What's this?

Chimeric Peptides of Statherin and Osteopontin That Bind Hydroxyapatite and Mediate Cell Adhesion^*

Michele Gilbert, Wendy J. Shaw^§, Joanna R. Long, Kjell Nelson, Gary P. Drobny^§, Cecilia M. Giachelli, and Patrick S. Stayton^¶

From the  Department of Bioengineering and ^§ Department of Chemistry, University of Washington, Seattle, Washington 98195

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_v melanoma cells when immobilized on the hydroxyapatite surface. Experiments with an integrin-sorted Mo_v subpopulation demonstrated that the _v3 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.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				M. Drobni, T. Li, C. Kruger, V. Loimaranta, M. Kilian, L. Hammarstrom, H. Jornvall, T. Bergman, and N. Stromberg Host-Derived Pentapeptide Affecting Adhesion, Proliferation, and Local pH in Biofilm Communities Composed of Streptococcus and Actinomyces Species Infect. Immun., November 1, 2006; 74(11): 6293 - 6299. [Abstract] [Full Text] [PDF]

				L. D. Niemi and I. Johansson Salivary Statherin Peptide-Binding Epitopes of Commensal and Potentially Infectious Actinomyces spp. Delineated by a Hybrid Peptide Construct Infect. Immun., February 1, 2004; 72(2): 782 - 787. [Abstract] [Full Text] [PDF]

				P. S. Stayton, G. P. Drobny, W. J. Shaw, J. R. Long, and M. Gilbert MOLECULAR RECOGNITION AT THE PROTEIN-HYDROXYAPATITE INTERFACE Critical Reviews in Oral Biology & Medicine, September 1, 2003; 14(5): 370 - 376. [Abstract] [Full Text] [PDF]