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Protein aggregation is a major pathological feature of neurodegenerative diseases such as Alzheimer`s disease (AD), Parkinson`s disease (PD), amyotrophic lateral sclerosis (ALS), and Huntington`s disease (HD). Under pathological conditions, Tau, Amyloid beta, alpha-synuclein, TDP-43, Huntingtin and other proteins integrate into a wide array of undesirable structures, ranging from oligomers and prefibrillar assemblies to highly ordered aggregates. The fibrillar structure represents a rapid growth phase of protein aggregation as these fibrils are “active” and rapidly recruit monomers for elongation. In additions, these fibrils randomly break into shorter fragments that could act as “seeds”, which transmits to other cells and independently recruits monomers to form novel fibrils.