The pathological process of neurodegenerative diseases, such as Alzheimer's disease, type 2 diabetes, Parkinson’s disease, etc., is closely related to the aggregation of one or more types of amyloid peptides. The amyloid peptides assemble into mature fibril undergoing misfolding, nucleation and elongation stages, and increasing evidences have shown that the neurotoxicity comes from the oligomerization and fibrillation. The formation of amyloid fibrils is influenced by multiple factors (e.g., peptide concentration, ionic strength, temperature, pH, membrane environment, etc.). Still, the dynamics of aggregation, structures of intermediate products, and related toxicity remain elusive. Exploring the aggregation of amyloid peptides and the achievement of effective modulation may facilitate the detection and mitigation of neurodegenerative diseases.
The goal of this Research Topic is to provide an update on the understanding of structural basis and molecular mechanism for amyloid peptide aggregation, with a special emphasis on new insights into the inhibition using nanoparticles, small molecules, metals, etc.
Original research papers, reviews, and short communications covering experimental, theoretical or computational aspects related to the current Research Topic are all warmly welcome. The areas covered by this Research Topic may include but are not limited to:
• Structural basis for the aggregation of amyloid peptides
• Phase separation involved in amyloid aggregation
• Comparison between different amyloid peptides
• Novel inhibitors including nanoparticles, small molecules, metal ions, etc.
• Misfolding and aggregation of amyloid peptides at membrane
• Ligand and amyloid peptide interaction
• Molecular mechanisms on the dynamics of amyloid oligomerization and fibrillation
Keywords: protein aggregation, protein-membrane interaction, protein-nanoparticle interaction, amyloid peptide, inhibitory mechanism
Important note: All contributions to this Research Topic must be within the scope of the section and journal to which they are submitted, as defined in their mission statements. Frontiers reserves the right to guide an out-of-scope manuscript to a more suitable section or journal at any stage of peer review.
