Abstract: Neurodegenerative diseases (NDs) are a growing health problem associated with a high burden due to destructive and long-term clinical effects. Cellular aggregations of misfolded proteins are the most common pathological hallmark of many late-onset NDs called proteinopathies including Parkinson’s disease (PD), Alzheimer’s disease (AD), tauopathies, amyotrophic lateral sclerosis (ALS), and polyglutamine (polyQ) expansion diseases such as Huntington’s disease (HD) and various spinocerebellar ataxias (SCA) such as SCA3 (Renna et al., 2010). Misfolded proteins can be generated by posttranslational conjugation (e.g., hyperphosphorylated tau in AD), or endoproteolytic cleavage (e.g., amyloid β peptides) or genetic mutations in specific proteins (such as HTT in HD, α-synuclein in PD, PrPC in prion disease and SOD1 and TDP-43 in ALS) leading to the formation of oligomers.