Hostname: page-component-76dd75c94c-lpd2x Total loading time: 0 Render date: 2024-04-30T09:52:56.888Z Has data issue: false hasContentIssue false

Cellular Interaction with Biomaterials Modified by Arg-Gly-Asp Containing Peptides

Published online by Cambridge University Press:  15 February 2011

James R. Glass
Affiliation:
Telios Pharmaceuticals, Inc., 2909 Science Park Rd., San Diego, CA. 92121
William S. Craig
Affiliation:
Telios Pharmaceuticals, Inc., 2909 Science Park Rd., San Diego, CA. 92121
Ken Dickerson
Affiliation:
Telios Pharmaceuticals, Inc., 2909 Science Park Rd., San Diego, CA. 92121
Michael D Pierschbacher
Affiliation:
Telios Pharmaceuticals, Inc., 2909 Science Park Rd., San Diego, CA. 92121
Get access

Abstract

Because cells can recognize and attach to short synthetic peptides containing the tripeptide sequence, arg-gly-asp (RGD), we have designed peptides which will spontaneously bind and present an active RGD sequence on biomaterial surfaces. We have analyzed a number of synthetic peptides and fully characterized one which fulfills this functional criteria. This peptide has been named PepTite-2000™. When biomaterials are placed in aqueous buffers containing PepTite-2000, the peptide rapidly binds to the surface and provides a site for cell attachment. Cell attachment occurs to PepTite-2000 coated materials by an RGD dependent mechanism using the αvβ3 integrin. This coating protocol is widely applicable, and the peptide will coat and promote cell attachment to all the commonly used biomaterials we have tested including dacron, teflon, titanium and silicone. Analysis of the soft tissue response to dacron implants coated with PepTite-2000 demonstrates that the coating results in more rapid tissue ingrowth and less giant cell recruitment around the implanted materials. These data demonstrate that PepTite-2000 can be used to modify biomaterial surfaces and present a more “natural” site for cell interactions.

Type
Research Article
Copyright
Copyright © Materials Research Society 1992

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

1. Pierschbacher, M.D. and Ruoslahti, E., Nature, 309 30 (1984)CrossRefGoogle Scholar
2. Albeda, S.M. and Buck, C.A., FASEB J. 4, 2868 (1990)Google Scholar
3. Ruoslahti, E. and Pierschbacher, M.D., Science 238, 491 (1987)Google Scholar
4. Hynes, R.O., Cell 48, 549 (1987)CrossRefGoogle ScholarPubMed
5. Pytela, R., Pierschbacher, M.D., Ruoslahti, E., Cell 40, 191 (1985)CrossRefGoogle ScholarPubMed
6. Pytela, R., Pierschbacher, M.D., Ruoslahti, R., Proc. Natl. Acad. Sci. U.S.A. 82, 5766 (1985)Google Scholar
7. Ruoslahti, E., Hayman, E.G., Pierschbacher, M.D., Engvall, E., Meth. Enzymology 82, 803 (1982)CrossRefGoogle Scholar
8. Pierschbacher, M.D. and Ruoslahti, E., J.Bio.Chem., 80 17294 (1987)CrossRefGoogle Scholar
9. Hubbell, J.A., Massia, S.P., Desai, N.P., Drumheller, P.D., Biotech. 9, 568 (1991)Google Scholar