Natural polyphenols are one of the most actively investigated categories of amyloid
inhibitors, and resveratrol has recently been reported to inhibit and remodel the human islet …

Atomic descriptions of peptide self-assembly are crucial to an understanding of disease-
related peptide aggregation and the design of peptide-assembled materials. Obtaining …

The amyloid-β peptides form amyloid fibrils which are associated with Alzheimer's disease.
Amyloid-β (29–42) is its C-terminal fragment and a critical determinant of the amyloid …

The pre-fibrillar stages of amyloid formation have been implicated in cellular toxicity, but
have proved to be challenging to study directly in experiments and simulations. Rational …

Low pH has a strong stabilising effect on the fibrillar assembly of amyloid β, which is
associated with Alzheimer's disease. The stabilising effect is already pronounced at pH 6.0 …

Understanding the structural and energetic requirements of non-fibrillar oligomer formation
harbors the potential to decipher an important yet still elusive part of amyloidogenic peptide …

There are synergistic effects of Aβ and tau protein in Alzheimer's disease. Aβ1–42 protofibril
seeds induce conversion of human tau protein into β-sheet-rich toxic tau oligomers …

Secondary nucleation pathways in which existing amyloid fibrils catalyze the formation of
new aggregates and neurotoxic oligomers are of immediate importance for the onset and …

Protein aggregation is associated with fatal neurodegenerative diseases, including
Alzheimer's and Parkinson's. Mapping out kinetics along the aggregation pathway could …

The aggregation of the Aβ peptide (Aβ1–42) to form fibrils is a key feature of Alzheimer's
disease. The mechanism is thought to be a nucleation stage followed by an elongation …