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Biologically-Based Self-Assembling Hydrogels

Published online by Cambridge University Press:  01 February 2011

Brandon L. Seal  and
Alyssa Panitch
Brandon L. Seal
Affiliation:
Department of Bioengineering, Arizona State University Tempe, AZ 85287-9709, U.S.A.
Alyssa Panitch
Affiliation:
Department of Bioengineering, Arizona State University Tempe, AZ 85287-9709, U.S.A.
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Abstract

We have developed polymers, which borrowing from biology, assemble into networks. The self-assembly regions of fibrinogen were cloned to form a scaffolding that either interacts with fibrin or assembles independently. Peptides consisting of a binding pocket (BP), ligand (L), and/or a Factor XIIIa substrate were synthesized and conjugated to methacroylated dextran or acrylated poly(ethylene glycol). Peptide-conjugated dextran was added to polymerizing fibrin, and the resulting hydrogels were evaluated rheologically. These conjugates significantly affected the mechanical properties of fibrin while the addition of unconjugated dextran did not. The BP and L peptides were conjugated to PEG star polymer. Mixtures of conjugated PEG-BP and PEG-L were found to assemble. This work shows that peptides directing assembly can be designed using motifs found in proteins. The peptides in this study not only alter the mechanical properties of fibrin, but also allow a mechanism for creating a self-assembling network.

Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 724: Symposium N – Biological and Biomimetic Materials Properties to Function , 2002 , N3.2
Copyright
Copyright © Materials Research Society 2002

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References

1. Petka, W. A., Harden, J. L., McGrath, K. P., Wirtz, D. and Tirrell, D. A.. Science 281: 389–392 (1998).Google Scholar
2. Wang, C., Stewart, R. J. and Kopecek, J.. Nature 397: 417–420 (1999).Google Scholar
3. Huang, S., Mulvihill, E. R., Farrell, D. H., Chung, D. W. and Davies, E. W.. J. Biol. Chem. 268(12): 8919–8926 (1993).Google Scholar
4. Xu, W.-f., Chung, D. W. and Davie, E. W.. J. Biol. Chem. 271(44): 27948–27953 (1996).Google Scholar
5. Zhang, J.-Z. and Redman, C. M.. J. Biol. Chem. 271(21): 12674–12680 (1996).Google Scholar
6. Shimizu, A., Nagel, G. M. and Doolittle, R. F.. Proc. Nat. Acad. Sci. 89: 2888–2892 (1992).Google Scholar
7. Horwitz, B. H., Varadi, A. and Scheraga, H. A.. Proc. Nat. Acad. Sci. 81: 5980–5984 (1994).Google Scholar
8. Cote, H. C. F., Pratt, K. P., Davie, E. W. and Chung, D. W.. J. Biol. Chem. 272(38): 23792–23798 (1997).Google Scholar
9. Olexa, S. A. and Budzynski, A. Z.. J. Biol. Chem. 256(7): 3544–3549 (1981).Google Scholar
10. Lorand, L., Parameswaren, K. N. and Murthy, S. N. P.. Proc. Nat. Acad. Sci. 95: 537–541 (1998).Google Scholar
11. van Dijk-Wolthuis, W., Steenbergen, M. van, Underberg, W. and Hennink, W.. J. Pharm. Sci. 86: 413–417 (1997).Google Scholar
12. Chambon, F. and Winter, H. H.. Pol. Bul. 13: 499–503 (1985).Google Scholar
13. Tung, C.-Y. M. and Dynes, P. J.. J. Appl. Poly. Sci. 27: 569–574 (1982).Google Scholar
14. Hastenberg, S., Panitch, A., Rizzi, S., Hall, H. and Hubbell, J. A.. Biomacromolecules In Press (2002).Google Scholar
15. Schense, J. C. and Hubbell, J. A.. Bioconj. Chem. 10(1): 75–81 (1999).Google Scholar