Despite advances in machine learning-based protein structure prediction, we are still far
from fully understanding how proteins fold into their native conformation. The conventional …

The possible link between hIAPP accumulation and β-cell death in diabetic patients has
inspired numerous studies focusing on amyloid structures and aggregation pathways of this …

Highlights•New structures have shown that there is a remarkable diversity and complexity of
the amyloid fold.•The same sequence forms different amyloid structures in different …

Unnatural helical peptidic foldamers have attracted considerable attention owing to their
unique folding behaviours, diverse artificial protein binding mechanisms, and promising …

Oligomers which form during amyloid fibril assembly are considered to be key contributors
towards amyloid disease. However, understanding how such intermediates form, their …

Metabolic disorders have become among the most serious threats to human health, leading
to severe chronic diseases such as obesity, type 2 diabetes, and non-alcoholic fatty liver …

Parkinson's disease (PD) is the most common neurological movement disorder
characterized by the selective and irreversible loss of dopaminergic neurons in substantia …

Aggregation of the peptide hormone amylin into amyloid deposits is a pathological hallmark
of type-2 diabetes (T2D). While no causal link between T2D and amyloid has been …

Chemotherapy has been validated unavailable for treatment of renal cell carcinoma (RCC)
in clinic due to its intrinsic drug resistance. Sensitization of chemo‐drug response plays a …

The conversion of otherwise soluble proteins into insoluble amyloid aggregates is
associated with a range of neurodegenerative disorders, including Alzheimer's and …