Dr Cassandra Terry
London Metropolitan University, UK.
Title: Structural characterisation of proteins involved in neurodegeneration
Biography
Biography: Dr Cassandra Terry
Abstract
Proteins need to maintain their correct structure in order to carry out specific biological functions. When proteins fold incorrectly (misfold) and are not cleared from the body, these proteins can accumulate and cause disease. Researching protein misfolding is crucial to understanding how misfolded proteins cause a number of debilitating and fatal diseases such as Alzheimer’s Disease, prion diseases (e.g. Creutzfeldt-Jakob disease), Parkinson’s disease and Type II Diabetes. There are no known cures or treatments for neurodegenerative disorders (such as Alzheimer’s or Parkinson’s disease) due to our limited understanding of protein misfolding mechanisms and the lack of detailed structures of these misfolded proteins. Recently however, much progress has been made in investigating the structures of some of these proteins using structural methods such as Cryo-Electron Microscopy (Cryo-EM) and Atomic Force Microscopy (AFM). Recent structures of misfolded prion proteins (PrP) isolated from prion-infected mammalian brain revealed a unique structure distinct from propagating assemblies of the Alzheimer’s proteins (amyloid-β, tau) and proteins involved in Parkinson’s disease (α-synuclein) that have been reported. More high-resolution structures of misfolded proteins involved in disease plus research into how and why proteins misfold are now urgently needed to move forward in developing future therapeutics.