β-sheet side chain polymers synthesized by atom-transfer radical polymerization

L. Ayres, P.H.H.M. Adams, D.W.P.M. Löwik, J.C.M. Hest, van

Research output: Contribution to journalArticleAcademicpeer-review

49 Citations (Scopus)

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 languageEnglish
Pages (from-to)825-831
Number of pages7
JournalBiomacromolecules
Volume6
Issue number2
DOIs
Publication statusPublished - Mar 2005
Externally publishedYes

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