Protein aggregation articles from across Nature Portfolio

More than a century after the first description of amyloids by Alois Alzheimer, and despite the enormous research efforts since then, the field is still full of surprises. While searching for answers to questions for example on the driving force, mechanism, and regulation of amyloidogenesis, or on the structure, physiological and pathological roles of different amyloid aggregates, unexpected properties are regularly revealed, broadening their application possibilities. This Collection aims to focus on the beneficial sides of amyloid formation, primarily exploring the potential use of amyloids in material science, bioengineering, and synthetic chemistry.

Aggregation of the RNA-binding protein TDP-43 is commonly observed in neurodegenerative disorders. A new study reveals that this process may be blocked by HSPB1, a small heat shock protein that can also regulate TDP-43 phase separation. This may be relevant to neurodegeneration, as loss of HSPB1 correlates with TDP-43 pathology.

The prion hypothesis embodies the radical concept that prion proteins contain the necessary information for infectious replication within their shape, thus obviating the requirement for genomic material. Two elegant papers by Hoyt et al. and Manka et al. describing high-resolution structures of infectious prions bring us closer to answering the long-standing question of how different prion conformations produce heritably distinct diseases.