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

Protein folding involves a large number of steps and conformations in which the folding
protein samples different thermodynamic states characterized by local minima. Kinetically …

Amyloid fibrils are supramolecular homopolymers of proteins that play important roles in
biological functions and disease. These objects have received an exponential increase in …

The development of atomic force microscopy (AFM) has opened up a wide range of novel
opportunities in nanoscience and new modalities of observation in complex biological …

Oligomeric forms of amyloid aggregates have been detected in the brains and tissues of
patients suffering from neurodegenerative disorders such as Parkinson's disease, and it is …

Proteinaceous deposits of α-synuclein amyloid fibrils are a hallmark of human disorders
including Parkinson's disease. The onset of this disease is also associated with five familial …

Amyloidogenic model peptides are invaluable for investigating assembly mechanisms in
disease related amyloids and in protein folding. During aggregation, such peptides can …

The self-assembly of protein molecules into highly ordered linear aggregates, known as
amyloid fibrils, is a phenomenon receiving increasing attention because of its biological …

In this chapter, we present an overview of the kinetics and thermodynamics of protein
aggregation into amyloid fibrils. The perspective we adopt is largely experimental, but we …