Nanofibrillar materials, such as cellulose, chitin and silk, are highly ordered architectures,
formed through the self-assembly of repetitive building blocks into higher-order structures …

Self-assembled peptide and protein amyloid nanostructures have traditionally been
considered only as pathological aggregates implicated in human neurodegenerative …

Amyloid-β (Aβ) is a 39–42 residue protein produced by the cleavage of the amyloid
precursor protein (APP), which subsequently aggregates to form cross-β amyloid fibrils that …

Background Protein aggregation correlates with the development of several debilitating
human disorders of growing incidence, such as Alzheimer's and Parkinson's diseases. On …

This review summarises our current understanding of the underlying and universal
mechanism by which newly synthesised proteins achieve their biologically functional states …

Recent reports give strong support to the idea that amyloid fibril formation and the
subsequent development of protein deposition diseases originate from conformational …

The presence of β‐sheets in the core of amyloid fibrils raised questions as to whether or not
β‐sheet‐containing proteins, such as transthyretin, are predisposed to form such fibrils …

Amyloid proteins have the ability to form insoluble fibril aggregates that have important
pathogenic effects in many tissues. Such amyloidoses are prominently associated with …

The self-assembly of amphiphilic peptides is reviewed. The review covers surfactant-like
peptides with amphiphilicity arising from the sequence of natural amino acids, and also …

Nanofiber structures of some peptides and proteins as biological materials have been
studied extensively, but their molecular mechanism of self-assembly and reassembly still …