Amyloids were conventionally referred to as extracellular and intracellular accumulation of
Aβ42 peptide, which causes the formation of plaques and neurofibrillary tangles inside the …

Hydrogels with inherent antibacterial activities have been attracting increasing attention,
particularly for biomedical applications. Biology provides a range of materials and …

DNA origami has created complex structures of various spatial dimensions. However, their
versatility in terms of function is limited due to the lower number of the intrinsic building …

Proteinaceous nanostructures have emerged as a promising strategy to develop safe and
efficient subunit vaccines. The ability of synthetic β-sheet self-assembling peptides to …

Amyloid-β (Aβ) is an intrinsically disordered peptide thought to play an important role in
Alzheimer's disease (AD). It has been the target of most AD therapeutic efforts, which have …

Different cellular and molecular changes underlie the pathogenesis of Alzheimer's disease
(AD). Among these, neuron‐specific dysregulation is a necessary event for accumulation of …

Protein aggregation into amyloid fibrils is associated with several amyloidoses, including
neurodegenerative Alzheimer's and Parkinson's diseases. Despite years of research and …

The assembly of amyloidogenic proteins into highly-structured fibrillar aggregates is related
to the onset and progression of several amyloidoses, including neurodegenerative …

Protein aggregation into amyloid fibrils is linked to multiple disorders. The understanding of
how natively non-harmful proteins convert to these highly cytotoxic amyloid aggregates is …

Prion diseases are fatal neurodegenerative diseases associated with structural conversion
of α-helical prion protein (PrP) into its β-sheet rich isoform (PrP Sc). Previous genetic …