Abstract
Silks are a widely studied class of naturally occurring structural proteins. Dragline spider silk, in particular, is considered to be nature's high-performance material due to its remarkable combination of strength and toughness. These mechanical properties stem from the protein secondary structure, a combination of well-defined β-sheets in a less well-defined glycine-rich matrix. The translation of this structure into a synthetic polymer was the aim of this investigation. To achieve this, a peptide-based monomer containing the sequence alanine - glycine - alanine - glycine, a well-known β-sheet-forming sequence found in silk, was synthesized. Using atom-transfer radical polymerization and a bifunctional initiator, a well-defined peptide-based polymer was prepared. This was then used as the macroinitiator for the polymerization of methyl methacrylate. The resulting well-defined triblock copolymer was analyzed using IR spectroscopy, which clearly showed β-sheet secondary structure had been introduced.
Original language | English |
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Pages (from-to) | 825-831 |
Number of pages | 7 |
Journal | Biomacromolecules |
Volume | 6 |
Issue number | 2 |
DOIs | |
Publication status | Published - Mar 2005 |
Externally published | Yes |