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Amyloid Cross-Seeding: Mechanism,Implication, and Inhibition
Authors:Sushma Subedi  Santanu Sasidharan  Niharika Nag  Prakash Saudagar  Timir Tripathi
Institution:1.Molecular and Structural Biophysics Laboratory, Department of Biochemistry, North-Eastern Hill University, Shillong 793022, India; (S.S.); (N.N.);2.Department of Biotechnology, National Institute of Technology Warangal, Warangal 506004, India;
Abstract:Most neurodegenerative diseases such as Alzheimer’s disease, type 2 diabetes, Parkinson’s disease, etc. are caused by inclusions and plaques containing misfolded protein aggregates. These protein aggregates are essentially formed by the interactions of either the same (homologous) or different (heterologous) sequences. Several experimental pieces of evidence have revealed the presence of cross-seeding in amyloid proteins, which results in a multicomponent assembly; however, the molecular and structural details remain less explored. Here, we discuss the amyloid proteins and the cross-seeding phenomena in detail. Data suggest that targeting the common epitope of the interacting amyloid proteins may be a better therapeutic option than targeting only one species. We also examine the dual inhibitors that target the amyloid proteins participating in the cross-seeding events. The future scopes and major challenges in understanding the mechanism and developing therapeutics are also considered. Detailed knowledge of the amyloid cross-seeding will stimulate further research in the practical aspects and better designing anti-amyloid therapeutics.
Keywords:amyloid proteins  aggregation  cross-seeding  protein misfolding diseases  dual inhibition  fibrillation
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