Alkaloid Biotransformations and Biomaterials from Short Amyloid Forming Peptides

We have an interest in industrial biotechnology and the use of enzymes to develop greener and cheaper routes for pharmaceutical production; this includes new semi-synthetic routes from agricultural feedstocks and methods to produce new lead compounds.  One enzyme superfamily with the ability to chemically modify and diversify lead candidates is the cytochrome P450s.  We have developed and screened a mutant enzyme library for enzymes capable of metabolising the anti-cancer alkaloid noscapine.  The most promising mutants are being applied in a biphasic whole-cell biotransformation process.

A second interest is the self-assembly of de novo designed or naturally occurring peptide sequences into amyloid fibrils; this includes variants of the TTR_105-115 peptide and the chaplins involved in biofilm formation by the bacteriaStreptomycetes coelicolor.  We have created hybrid biomaterials from self-assembling synthetic DNA and peptides that organise onto predefined two-dimensional platforms via DNA–DNA hybridization interactions.  Our studies have tracked peptide assembly in solution and at the air-water interface and examined the interaction between fibrils and mammalian cells to better understand the assembly and potential of such peptide systems.