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Updated: Jan 28, 2026

Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo
Published on: June 2, 2019
Cryo-Electron Microscopy Uncovers Key Residues within the Core of Alpha-Synuclein Fibrils
Ritobrita Chakraborty1, Krishnananda Chattopadhyay1
1Protein Folding and Dynamics Laboratory, Structural Biology and Bioinformatics Division , CSIR-Indian Institute of Chemical Biology , 4, Raja Subodh Chandra Mullick Road , Kolkata 700032 , India.
Abstract:
Recent expeditious advances in the determination of the 3-D structure of fibrils of alpha-synuclein, the intrinsically disordered protein associated with the neurodegenerative Parkinson's disease (PD), have identified amino acid contacts that form the fibril's inter-protofilament interface. The residues that constitute this "steric zipper" interface determine the morphology of the fibrils as well as toxicity of the oligomeric building units or "kernels" which lead to the formation of the protofilaments. The zipper interface houses key amino acid residues involved in familial PD that can be targeted by drug design.
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