Abstract
Chaperones assist in maintenance of functional proteome in vivo. However, they seem to be either ineffective or overwhelmed in the case of protein misfolding diseases like Parkinson's, Huntington's or Alzheimer's. Studies involving one or two chaperones from Hsp70 system cannot provide comprehensive information about the involvement of whole system. We present for the first time, in vitro characterization of the effect of each component of Hsp70 system on α-synuclein (involved in Parkinson's) using SEC and ThT assay. Our results show while some components enhance the aggregation others seem to stabilize α-synuclein against aggregation. Keeping whole Hsp70 system intact, the factor responsible for triggering aggregation seemed to be initial α-synuclein conformation.
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