The mechanistic characterisation of misfolding proteins in disease and cancer therapy

Abstract

Protein folding is a highly ordered and governed event which results in the production of native peptide structures capable of carrying out a myriad of functions and processes within the cell. Failure to produce fully folded proteins was thought to result in toxic entities which have been associated with numerous degenerative disorders such as Alzheimer’s disease. Despite significant advances, the molecular identity of the cytotoxic species populated during in vivo amyloid formation crucial for the understanding of neurodegenerative and other systemic amyloidosis is yet to be revealed. Importantly not all protein misfolding has a negative outcome.