P44: De novo peptide self-assembly for antimicrobial and gene delivery strategies
Supervisors: Professor Franca Fraternali (KCL, Faculty of Life Sciences and Medicine, Randall Division of Cell & Molecular Biophysics) and Dr Chris Lorenz (KCL, Faculty of Natural & Mathematical Sciences, Department of Physics)
Industry Supervisor: Dr Max Ryadnov (National Physical Laboratory)
Peptide self-assembly is being exploited for the construction of nano-to-micro scale assemblies from the bottom up. Peptides can be readily made and their sequences are structurally amendable to support specialist functions ranging from tissue repair to antimicrobial activity. Establishing the physicochemical determinants that underlie peptide self-assembly as a process and a tool is an essential step towards novel applications in biomedicine.
Combining computational methods with experimental biophysical approaches provides a powerful strategy for the development of a framework aiding in the better understanding of mechanisms behind the formation of self-assembled structures and in their designs possessing selected properties.
In this context, researchers from the National Physical Laboratory (NPL) led by Max Ryadnov apply the principles of de novo protein design to construct artificial peptide sequences that assemble into novel macromolecular architectures with different functions enabling intracellular delivery and antimicrobial activity.
These are experimental designs but are best described using computer molecular dynamics simulations which allow deciphering, with atomistic precision, the exact self-assembly mechanisms. Importantly, interactions in a specific environment in which the designed peptides and their assemblies exploit their function can be modelled and detailed in silico. In this project we will demonstrate how the first design principles of self-assembling peptides can be used and computationally prescribed to lead to novel and efficient antimicrobial and gene delivery strategies.