Polymer protein hybrids

Structural proteins form an important source of inspiration for materials scientists, because of the well-defined relationship between their three-dimensional folding pattern and their physical properties. Incorporation of structural peptide elements in synthetic polymers allows the combination of natural structural control with synthetic versatility. In this report, two approaches to introduce silk-inspired β-sheot elements in hybrid block copolymers are described. In our first approach we have successfully applied the controlled radical polymerization technique Atom Transfer Radical Polymerization (ATRP) to construct ABA triblock copolymers, of which the A blocks consist of PMMA and the B block consists of Ala-Gly-Ala-Gly-methacrylate moieties. This method leads to triblock copolymers with the structural peptide elements in the side chain of the middle block. Our second approach uses protein engineering for the construction of the β-sheet element. The latter is converted into a triblock copolymer architecture by modification of both the N and C ends with poly(ethylcneglycol) chains, In this case the B block consists solely of the β-sheet peptide element. It was demonstrated that it is possible to introduce β-sheet characteristics in the hybrid material by means of both approaches.