Protein amyloid aggregation is associated with multiple diseases including well-known Alzheimer’s and Parkinson’s, as well as infectious prion diseases. Prion-like self-replication of fibrils in vitro (termed “seeding”) is a common feature for many amyloid-forming proteins and there is growing evidence of prion-like spreading of amyloids in vivo. Moreover, emerging data suggests that cross-seeding and other cross-interactions between different amyloid-forming proteins may play an important role in the progress of amyloid-related diseases. Inability to account for these interactions in development of anti-amyloid drugs may be one of the reasons why the best developed lead molecules fail in clinical trials.
The goal of this Research Topic is to expand the understanding the role of interactions between different proteins and peptides in the process of protein amyloid formation.
Both original research papers and reviews, covering experimental, theoretical, or computational aspects related to the current Research Topic are welcome. The areas covered by this Research Topic may include but are not limited to:
• Interactions between different amyloid forming proteins
• Interactions between different isoforms of the same protein
• Interactions between different mutants of the same protein
• Interactions between the protein and it’s fragment peptides
• Interactions between same proteins from different species
We also encourage to report negative data (for example if you tested hypothesis of interactions between amyloid-forming proteins A and B and conclude no interactions).
Dr. Rita PY Chen holds patents related to this Research Topic
Dr. Michal Burdukiewicz holds patents related to this Research Topic, and is the CEO and Founder of the private company '.Prot.'.
All other Topic Editors declare no Conflict of Interest.
Protein amyloid aggregation is associated with multiple diseases including well-known Alzheimer’s and Parkinson’s, as well as infectious prion diseases. Prion-like self-replication of fibrils in vitro (termed “seeding”) is a common feature for many amyloid-forming proteins and there is growing evidence of prion-like spreading of amyloids in vivo. Moreover, emerging data suggests that cross-seeding and other cross-interactions between different amyloid-forming proteins may play an important role in the progress of amyloid-related diseases. Inability to account for these interactions in development of anti-amyloid drugs may be one of the reasons why the best developed lead molecules fail in clinical trials.
The goal of this Research Topic is to expand the understanding the role of interactions between different proteins and peptides in the process of protein amyloid formation.
Both original research papers and reviews, covering experimental, theoretical, or computational aspects related to the current Research Topic are welcome. The areas covered by this Research Topic may include but are not limited to:
• Interactions between different amyloid forming proteins
• Interactions between different isoforms of the same protein
• Interactions between different mutants of the same protein
• Interactions between the protein and it’s fragment peptides
• Interactions between same proteins from different species
We also encourage to report negative data (for example if you tested hypothesis of interactions between amyloid-forming proteins A and B and conclude no interactions).
Dr. Rita PY Chen holds patents related to this Research Topic
Dr. Michal Burdukiewicz holds patents related to this Research Topic, and is the CEO and Founder of the private company '.Prot.'.
All other Topic Editors declare no Conflict of Interest.