ORGN 236 |
| Joel P Schneider, Chemistry and Biochemistry, Chemistry and Biochemistry, University of Delaware, Newark, DE 19716 |
| Peptide design has been used to construct chemically and mechanically responsive materials. A general peptide design is presented that links the intramolecular folding of beta-hairpin peptides to their propensity to self-assemble affording hydrogels rich in beta-sheet. Peptide folding and thus consequent self-assembly leading to hydrogel material can be triggered by changes in solution pH, ionic strength, exposure to light, or temperature. Depending on the environmental trigger employed, folding and self-assembly events can be totally reversible affording "smart" materials responsive to their environment. CD, IR, rheology, neutron scattering, confocal microscopy and TEM experiments show that hydrogels formed from these peptides are rich in beta-sheet structure, well hydrated on both the nano- and micro- length scales, and are microporous yet mechanically rigid. Thorough characterization of the gelation process suggests that by linking the intramolecular folding of small designed peptides to their ability to self-assemble, responsive materials can be prepared. Importantly, bulk material properties of the hydrogel such as rigidity can be predictably modulated via peptide design. The utility of these materials in tissue reconstruction is initially explored via cytocompatibility experiments that demonstrate that the nano and microstructure of the hydrogel scaffold fosters cell adhesion and proliferation of model fibroblasts. |
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Molecular Recognition and Self-Assembly
8:00 AM-12:00 PM, Monday, August 23, 2004 Pennsylvania Convention Center -- 201B, Oral
Division of Organic Chemistry |