Transthyretin amyloidosis is a fatal disorder that is characterized primarily by progressive
neuropathy and cardiomyopathy. It occurs in both a mutant form (with autosomal dominant …

The aggregation of a polypeptide chain into amyloid fibrils and their accumulation and
deposition into insoluble plaques and intracellular inclusions is the hallmark of several …

Systemic ATTR amyloidosis is an increasingly important protein misfolding disease that is
provoked by the formation of amyloid fibrils from transthyretin protein. The pathological and …

Measurement of the average intensity of excess scattering, termed static light scattering
(SLS), has become one of the most widely used techniques for the determination of molar …

Protein misfolding and aggregation have attracted immense research interests due to their
connection with an array of degenerative diseases including neurodegenerative disorders …

Highly ordered, straight amyloid fibrils readily lend themselves to structure determination
techniques and have therefore been extensively characterized. However, the less ordered …

Inhibition of fibril formation is considered a possible treatment strategy for amyloid-related
diseases. Understanding the molecular nature of inhibitor action is crucial for the design of …

Protein aggregation and subsequent accumulation of insoluble amyloid fibrils with cross-β
structure is an intrinsic characteristic of amyloid diseases, ie, amyloidoses. Amyloid …

Aggregation of transthyretin (TTR) is the causative agent for TTR cardiomyopathy and
polyneuropathy amyloidoses. Aggregation is initiated by dissociation of the TTR tetramer …

Transthyretin (TTR) aggregation via misfolding of a mutant or wild-type protein leads to
systemic or partial amyloidosis (ATTR). Here, we utilized variable biophysical assays to …