POLY 433 |
| Materials made from proteins have been the focus of research efforts for some time. Silks, in particular, have a well defined alternating crystalline and amorphous block in their primary sequence, which suggests the use of multiblock copolymer architectures as viable biomimetic models. Herein we report the synthesis of B. mori silk-based materials in which the β-sheet forming region is approximated by AGAG, AGAGSG and GAGAGS while the amorphous reign is substituted with poly(ethylene glycol). From conformational analysis of the polymers it is found that the peptide units form β-sheets resembling those in the native silk. Stress-strain data indicate the polymer is much tougher than any silk-based polymer to date, with elongation at break exceeding 300-600 percent in certain cases. Detail studies of such synthetic biopolymer models are expected to provide valuable insight into the factors governing self-assembly and nanostructure formation in native biopolymers. |
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7th International Biorelated Polymers Symposium
6:00 PM-8:00 PM, Tuesday, 12 September 2006 Moscone Center -- Hall D, Poster
Sci-Mix
Division of Polymer Chemistry |