Langmuir monolayers at the air/water interface have been used for decades to mimic cell
membranes in attempts to determine the mechanisms behind the physiological action of …

Alpha synuclein (αS) is a~ 14 kDa intrinsically disordered protein. Decades of research have
increased our knowledge on αS yet its physiological function remains largely elusive. The …

The aggregation of human α-Synuclein (α-Syn) into amyloid fibrils is related to the onset of
multiple diseases termed synucleinopathies. Substantial evidence suggests that …

Recent advances in the structural biology of disease-relevant α-synuclein fibrils have
revealed a variety of structures, yet little is known about the process of fibril aggregate …

Background β-Cell death is the key feature of type 2 diabetes mellitus (T2DM). The
misfolding of human Islet Amyloid Polypeptide (hIAPP) is regarded as one of the causative …

Loss of β-cell function and β-cell death is the key feature of type 2 diabetes mellitus (T2DM).
One hypothesis for the mechanism of this feature is amyloid formation by the human islet …

A large number of pathological diseases are known now to be associated with the
misfolding and the aberrant oligomerization and deposition of peptides and proteins into …

The misfolding of α-synuclein (αS) into amyloid aggregates is catalyzed by hydrophobic
surfaces and associated with severe brain disorders, such as Parkinson's disease. Despite …

Abstract Alpha-synuclein (α-syn) aggregation and mitochondrial dysfunction are considered
as two of the main factors associated with Parkinson's disease (PD). In the present …

Amyloid fibrils formed by the α‐Synuclein (α‐Syn) protein are the pathological hallmark of
multiple human disorders, generally termed α‐synucleinopathies. The aggregation process …