PMSE 131 |
| One of the advantages self-assembling nanomaterials have over static covalent ones is the ability to adapt or react in a productive fashion to the environment in which they are placed. Ideally a material could be designed with control over when, where and to what extent self-assembly happens independently of function of the material. Towards these goals we have developed a series symmetric multidomain peptides with the general block structure ABCBA in which the driving force for self-assembly - hydrophobic packing and hydrogen bonding - is contained within the C block. Control over the condition under which self-assembly takes place, and to a lesser extent its degree, is controlled by the highly charged B block. Finally, the applied chemical functionality of the material is contained in the flanking A blocks. The self-assembling system is characterized by infrared spectroscopy, circular dichroism and transmission electron microscopy. Based on these characterization methods we are able to draw correlations between the molecular conformation of the assembler, the resulting nanostructure and biological properties each of which can be tuned by modifying the respective block for that function. We demonstrate how these peptides can be used to easily entrap cells in a three dimensional matrix which can support and direct cell growth. |
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Designed Macromolecular Assemblies for Biomedical Applications
1:40 PM-5:20 PM, Monday, March 26, 2007 McCormick Place South -- Room S505B, Level 5, Oral
Division of Polymeric Materials: Science & Engineering |