ABSTRACT
Protein folding is one of the fundamental processes in living organism where linear proteins self assemble into their correct three-dimensional or “native” structure in order to carry out essential biological functions (Dobson 2003). Under normal circumstances, a protein will fold effi ciently and spontaneously into its intended structure often with the help of molecular chaperones. However, proteins that do not fold properly tend to misfold or aggregate, thus rendering the protein inactive and sometimes dysfunctional (Dobson 2003; Agorogiannis et al. 2004). Many natively unfolded proteins such as beta amyloid (A-beta) and alphasynuclein (a-syn) lack secondary structure and have a higher propensity to misfold and aggregate into fi brillar amyloid structures known as plaques. Aggregation and accumulation of plaques can disrupt other cellular components which may impair cellular function. Misfolded protein aggregates are a central component in many neurodegenerative diseases including Alzheimer’s disease (AD), Parkinson’s disease (PD), Huntington’s disease (HD), Creutzfeldt-Jakob diseases (CJD), and transmissible spongiform encephalopathies (TSEs).
