Disrupted protein folding or decreased protein stability can lead to the accumulation of
(partially) un‐or misfolded proteins, which ultimately cause the formation of protein …

This review is aimed to provide a concise yet extensive survey of key short bioactive peptide
sequences for a range of applications ranging from biomaterials development to peptides …

This review is concerned with the role of fibrillization of the amyloid β (Aβ)-peptide in
Alzheimer's disease (AD). The perspective is that of a physical chemist, and one aim is to …

The accumulation of β-sheet–rich amyloid fibrils or aggregates is a complex, multistep
process that is associated with cellular toxicity in a number of human protein misfolding …

Background Protein aggregation correlates with the development of several debilitating
human disorders of growing incidence, such as Alzheimer's and Parkinson's diseases. On …

Protein aggregation results in β-sheet–like assemblies that adopt either a variety of
amorphous morphologies or ordered amyloid-like structures. These differences in structure …

Amyloid-beta (Aβ) aggregates are the main constituent of senile plaques, the histological
hallmark of Alzheimer's disease. Aβ molecules form β-sheet containing structures that …

The global public health threat of antimicrobial resistance has led the scientific community to
highly engage into research on alternative strategies to the traditional small molecule …

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 …

Simple polyglutamine (polyQ) peptides aggregate in vitro via a nucleated growth pathway
directly yielding amyloid-like aggregates. We show here that the 17-amino-acid flanking …