Control and analysis of protein aggregation is an increasing challenge to pharmaceutical
research and development. Due to the nature of protein interactions, protein aggregation …

The fibrillization of peptides is relevant to many diseases based on the deposition of
amyloids. The formation of fibrils is being intensively studied, especially in terms of …

Here, we use single-molecule techniques to study the aggregation of α-synuclein, the
protein whose misfolding and deposition is associated with Parkinson's disease. We identify …

The conversion of proteins from their native state to misfolded oligomers is associated with,
and thought to be the cause of, a number of human diseases, including Alzheimer's disease …

Protein aggregation is one of the key challenges in the development of protein
biotherapeutics. It is a critical product quality issue as well as a potential safety concern due …

The all-α helix multi-domain protein bovine serum albumin (BSA) aggregates at elevated
temperatures. Here we show that these thermal aggregates have amyloid properties. They …

Amyloids are filamentous protein deposits ranging in size from nanometres to microns and
composed of aggregated peptide β-sheets formed from parallel or anti-parallel alignments of …

Understanding the structure, functionalities and biology of functional amyloids is an issue of
emerging interest. Inclusion bodies, namely protein clusters formed in recombinant bacteria …

Increasing evidence indicates that oligomeric protein assemblies may represent the
molecular species responsible for cytotoxicity in a range of neurological disorders including …

A number of medical disorders, including Alzheimer's disease and type II diabetes, is
characterised by the deposition of amyloid fibrils in tissue. The insolubility and size of the …