The formation of amyloid fibrils is a general class of protein self-assembly behaviour, which
is associated with both functional biology and the development of a number of disorders …

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 …

The formation of nanoscale amyloid fibrils from normally soluble peptides and proteins is a
common form of self-assembly phenomenon that has fundamental connections with …

Alzheimer's disease is a neurodegenerative disorder associated with the aberrant
aggregation of the amyloid-β peptide. Although increasing evidence implicates cholesterol …

Proteins at interfaces play important roles in cell biology, immunology, bioengineering, and
biomimetic material design. Many biological processes are based on interfacial protein …

Abstract α-synuclein is a small protein abundantly expressed in the brain and mainly located
in synaptic terminals. The conversion of α-synuclein into oligomers and fibrils is the hallmark …

Protein liquid–liquid phase separation can lead to disease-related amyloid fibril formation.
The mechanisms of conversion of monomeric protein into condensate droplets and of the …

Parkinson's disease (PD) is characterized by proteinaceous aggregates named Lewy
Bodies and Lewy Neurites containing α-synuclein fibrils. The underlying aggregation …

Understanding how normally soluble peptides and proteins aggregate to form amyloid fibrils
is central to many areas of modern biomolecular science, ranging from the development of …

It is increasingly recognized that molecular chaperones play a key role in modulating the
formation of amyloid fibrils, a process associated with a wide range of human disorders …