Targeting the infectious potential of prion and prion-like pathogens

"This project will develop a new cross-disciplinary method, involving a supramolecular chemical biology approach, for control/inhibition of prion and prion-like amyloid propagation. Protein aggregation is a general molecular phenomenon of great interest due to the wide range of diseases it is associated with. The diseases associated with protein aggregation, such as Alzheimer's and prion diseases also stand as unmatched global challenges: to date there is no reliable way to control the amyloid aggregation of proteins, which typically results in a very broad distribution of aggregate sizes and shapes, some will corrupt normally soluble and functional protein to propagate the amyloid state. Templation of synthetic polymers to control their size has been demonstrated using a base-pairing strategy, as has the interaction of nucleobase-functionalised peptides with their complementary bases. We propose to apply these strategies to make designer protein molecules that are able to control or inhibit amyloid protein aggregation and their propagation by size control.