Amyloid Hetero-Aggregation 2.0

Dear Colleagues,

This Special Issue will address the molecular and cellular mechanisms of amyloid hetero-aggregation, deposition, and toxicity of various proteins–human, bacterial, and viral. Studies conducted in vitro, in vivo, and ex vivo materials are welcome. Amyloid formation is a widespread phenomenon due to in the generic property of polypeptide chains that self-assemble into cross-β-sheet superstructures and are manifested in numerous amyloid-related diseases, as well as in functional amyloids. The amyloid cascade lies at the center of amyloid disease pathology, involved in up to 50 human diseases, though it is still debated if this is the cause or a consequence of disease. Amyloid formation in neurodegenerative disease and others is often associated with inflammation as a common denominator of those diseases. For example, inflammation triggers the massive production of proinflammatory S100A9 that spontaneously form amyloids and co-aggregates into hetero-amyloids together with Abeta or alpha-synuclein in Alzheimer’s or Parkinson’s disease, respectively. These events initiate the whole pathological amyloid cascade. Recently, the comorbidity of amyloid diseases was also shown to be linked to the co-aggregation of different amyloidogenic proteins. Since amyloids formed by individual polypeptides are highly polymorphic, their co-aggregates add up to the complexity and heterogeneity of the amyloid mixture. Despite the key clinical importance of amyloid formation, the mechanisms of co-aggregation of different amyloid species remain elusive. There is an unmet need to understand the architecture and mechanisms of self-assembly leading to the formation of hetero-aggregates composed of various amyloid polypeptides. Your research and review articles on this subject are very welcome in this issue.

Dr. Ludmilla A. Morozova-Roche
Guest Editor

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• amyloid
• co-aggregation
• hetero-aggregation
• human proteins
• bacterial amyloids
• viral proteins
• cytotoxicity
• structure
• function