Abrupt aggregation of misfolded proteins is a hallmark of a large number of severe
pathologies, including diabetes types 1 and 2, Alzheimer, and Parkinson diseases. A …

Spontaneous aggregation of misfolded proteins typically results in the formation of
morphologically and structurally different amyloid fibrils, protein aggregates that are strongly …

The misfolding and aggregation of human islet amyloid polypeptide (hIAPP) at cell
membrane has a close relationship with the development of type 2 diabetes (T2DM). This …

Human insulin has long been known to form amyloid fibrils under given conditions. The
molecular basis of insulin aggregation is relevant for modeling the amyloidogenesis …

Amyloid fibrils are β-sheet-rich protein aggregates commonly found in the organs and
tissues of patients with various amyloid-associated diseases. Understanding the structural …

Abnormal aggregation of islet amyloid polypeptide (IAPP) into amyloid fibrils is a hallmark of
type 2 diabetes. In this study, we investigated the initial oligomerization and subsequent …

Amyloid oligomers and fibrils are protein aggregates that cause an onset and progression of
many neurodegenerative diseases, diabetes type 2 and systemic amyloidosis. Although a …

Abrupt aggregation of amyloid beta (Aβ) peptide is strongly associated with Alzheimer's
disease. In this study, we used atomic force microscopy–infrared (AFM-IR) spectroscopy to …

Amyloid plaques are one of the central manifestations of Alzheimer's disease pathology.
Aggregation of the amyloid beta (Aβ) protein from amorphous oligomeric species to mature …

A model cosolvent, ethanol, has profound and diversified effects on the amyloidogenic self-
assembly of insulin, yielding spectroscopically and morphologically distinguishable forms of …