Beta-sheet side chain polymers synthesized by atom-transfer radical polymerization.
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 beta-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 beta-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 beta-sheet secondary structure had been introduced.
Ayres
Lee
L
Organic Chemistry Department, Institute for Molecules and Materials (IMM), Radboud University Nijmegen, Toernooiveld 1, Nijmegen 6525 ED, The Netherlands.
Adams
P Hans H M
PH
Löwik
Dennis W P M
DW
van Hest
Jan C M
JC
D004151:Dipeptides / Q000737:chemistry; D020366:Methylmethacrylate; D008968:Molecular Conformation; D009842:Oligopeptides / Q000737:chemistry*; D011108:Polymers / Q000138:chemical synthesis* / Q000737:chemistry; D017433:Protein Structure, Secondary; D017550:Spectroscopy, Fourier Transform Infrared
D004151:Dipeptides; D009842:Oligopeptides; D011108:Polymers; D020366:Methylmethacrylate; C028872:alanylglycine