Alpha-Synuclein Amyloid Fibril Formation: New Molecular Perspectives
A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".
Deadline for manuscript submissions: closed (30 September 2024) | Viewed by 3775
Special Issue Editor
Interests: amyloid fibril; protein aggregation; secondary structure; β-sheet; amide II; amyloids; prion proteins; fibril structure; s100a9; synuclein; amyloid proteins; fibrils; FTIR; AFM
Special Issue Information
Dear Colleagues,
Alpha-synuclein is linked with multiple neurodegenerative disorders, including Parkinson‘s disease, dementia with Lewy bodies, and multiple-system atrophy. It is also known to be associated with amyloid plaques found in patients suffering from Alzheimer‘s disease. Investigations into the subject of alpha-synuclein amyloid aggregation have demonstrated the protein’s ability to form multiple structurally diverse fibril strains and suggested their link with distinct synucleinopathies. These alpha-synuclein strains carry diverse levels of seeding, propagation, and neurotoxicity potential. Therefore, an immense amount of effort has been dedicated towards deciphering the underlying factors which determine this prion-like structural variability, including genetic mutations, environmental conditions, co-interactions with other proteins, and the recent discovery of liquid–liquid phase separation of alpha-synuclein. Despite tremendous progress in this field, there are still various unknown or unexplored factors regarding the transition from native state alpha-synuclein to its pathogenic variants. The purpose of this Special Issue is to collect scientific articles and reviews that can provide new molecular perspectives in the field of alpha-synuclein amyloid fibril formation.
Dr. Mantas Žiaunys
Guest Editor
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Keywords
- alpha-synuclein
- amyloid
- protein aggregation
- synucleinopathies
- protein fibrils
- protein misfolding
- prion-like
- protein-protein interactions
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