Abstract
This thesis describes the preparation, via atom transfer radical polymerisation (ATRP), of a series of peptide-polymer hybrid materials. The first chapter gives an overview of the work done so far in the preparation of peptide-polymer hybrid materials. In the second, third and fourth chapter, the controlled radical polymerisation, using ATRP, of peptide sequences based on the structural proteins silk and elastin was investigated. It was found that by including peptides sequences from these two structural proteins into the side chain of a synthetic polymer, the secondary structure associated with these peptide sequences was also introduced. In the case of the elastin based polymer a variety of interesting properties were observed. In the fifth chapter a beta-hairpin forming peptide, again based on silk, was used to initiate the polymerisation of methyl methacrylate. This gave rise to a triblock copolymer with a hydrophilic peptide as a central block with two hydrophobic outer blocks. Upon examining this polymer with electron microscopy large spherical aggregates were observed. In the final chapter a two monomers based on the antimicrobial peptides, KFFKFFKFFK and gramicidin S, a large cyclic decapeptide were prepared and polymerised using ATRP. The work done in this thesis demonstrates that it is possible to prepare peptide polymer hybrid materials in a controlled manner via ATRP. The combining of polymers and peptides in this way allows the preparation of novel materials with interesting and well defined secondary structures.
