Protein misfolding and aggregation can be induced by a wide variety of factors, such as
dominant disease-associated mutations, changes in the environmental conditions (pH …

Understanding the atomistic resolution changes during the self-assembly of amyloid
peptides or proteins is important to develop compounds or conditions to alter the …

The oligomers formed during the early steps of amyloid aggregation are thought to be
responsible for the neurotoxic damage associated with Alzheimer's disease. It is therefore of …

Proteins unfold in chaotropic salt solutions, a process that is difficult to observe at the single
protein level. The work presented here demonstrates that a liquid-based atomic force …

The formation of amyloid β (1-42)(Aβ42) oligomers is considered to be a critical step in the
development of Alzheimer's disease (AD). However, the mechanism underlying this process …

This review is focused on the atomic force microscopy (AFM) capabilities to study the
properties of protein biomolecules and to detect the proteins in solution. The possibilities of …

α-Synuclein (α-syn) is the major component of the intraneuronal inclusions called Lewy
bodies, which are the pathological hallmark of Parkinson's disease. α-Syn is capable of self …

Background Aggregation of the neuronal protein α-synuclein into amyloid fibrils is a
hallmark of Parkinson's disease. The propensity of α-synuclein to aggregate increases with …

Alzheimer's disease (AD) and Parkinson's disease (PD) are the two most common
neurodegenerative disorders, characterized by aggregation of amyloid polypeptides, β …

Oligomer formation of amyloid-β peptides (Aβ) is accelerated at a hydrophilic/hydrophobic
interface. However, details of the acceleration mechanism have not been elucidated. To …