Amyloid suprastructure-function relationships: Polymorphism, stability, toxicity and infectious potential Seminar

Speaker information

Dr Wei-Feng Xue, University of Kent. Amyloid structures consist of highly ordered forms of protein assembled from whole or parts of normal soluble proteins or peptides of diverse amino acid sequences. The devastating human diseases associated with amyloid, such as Alzheimer's disease, Creutzfeldt-Jakob (CJD prion disease), Huntington's disease, Parkinson disease, type II diabetes mellitus, and systemic amyloidosis, are linked to the way the amyloid structures are assembled and deposited in the brain or in other parts of the human body. But far from all amyloid assemblies are disease-associated, as some amyloid fibrils have also been recognised as a class of functional protein assemblies, which can play a number of important roles in bacteria, yeast and humans. A sub-class of amyloid can spread between organisms by forming small seeds through the breakage of larger fibrils. These are called prions, and they exist in humans where they cause prion diseases such as CJD. In yeast, prions confer special cellular properties in yeast cells that are passed on from generation to generation, as a form of epigenetic or 'protein gene'. Amyloid fibrils are defined by their cross-beta core structure, where continuous beta-sheets run through the core of amyloid fibrils perpendicularly to the fibril axis. My research is focused on resolving the fundamental mechanisms that govern the formation and the molecular lifecycle of amyloid protein aggregates. The long-term research vision in my lab is to fully understand the assembly of protein fibrils, as well as how different mechanisms involved in amyloid assembly are linked to the disease-associated properties and useful biological functions of amyloid.