Natural biomolecular systems have evolved to form a rich variety of supramolecular
materials and machinery fundamental to cellular function. The assembly of these structures …

The phenomenon of protein aggregation and amyloid formation has become the subject of
rapidly increasing research activities across a wide range of scientific disciplines. Such …

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

The generation of toxic oligomers during the aggregation of the amyloid-β (Aβ) peptide Aβ42
into amyloid fibrils and plaques has emerged as a central feature of the onset and …

The cellular processes underpinning life are orchestrated by proteins and their interactions.
The associated structural and dynamic heterogeneity, despite being key to function, poses a …

Nucleation of new peptide and protein aggregates on the surfaces of amyloid fibrils of the
same peptide or protein has emerged in the past two decades as a major pathway for both …

Mechanical interlocking of molecules (catenation) is a nontrivial challenge in modern
synthetic chemistry and materials science,. One strategy to achieve catenation is the design …

Alzheimer's disease (AD) is the primary cause of age-related dementia. Effective strategies
to prevent and treat AD remain elusive despite major efforts to understand its basic biology …

The formation of amyloid fibrils by the intrinsically disordered protein α-synuclein is a
hallmark of Parkinson disease. To characterize the microscopic steps in the mechanism of …

Abstract α-Synuclein (α-syn) is a 140-residue intrinsically disordered protein that is involved
in neuronal and synaptic vesicle plasticity, but its aggregation to form amyloid fibrils is the …