The aggregation and deposition of the amyloid-β peptide (Aβ) in the brain has been linked
with neuronal death, which progresses in the diagnostic and pathological signs of …

The native structure of proteins is central to various functions performed by cells. A vital part
of the structure-function paradigm of proteins is their inherent flexibility and dynamics. The …

The aggregation of amyloidogenic proteins is infamous for being highly chaotic, with small
variations in conditions sometimes leading to large changes in aggregation rates. Using the …

In the commonly used nucleation-dependent model of protein aggregation, aggregation
proceeds only after a lag phase in which the concentration of energetically unfavorable …

The clearance of overloaded amyloid β (Aβ) oligomers is thought to be an attractive and
potential strategy for the therapy of Alzheimer's disease (AD). A variety of strategies have …

Using NMR to probe transient binding of Aβ1–40 monomers to fibers, we find partially bound
conformations with the highest degree of interaction near F19–K28 and a lesser degree of …

The deposition of aggregates of human islet amyloid peptide (hIAPP) has been correlated
with the death of insulin-producing beta (β) cells in type II diabetes mellitus. The actual …

Fluorinated amino acids can have dramatic effects on protein stability and protein–protein
interactions due to the unique stereoelectronic properties of fluorine. Previous approaches …

We herein report the mechanism of amyloid formation of amyloid-β (Aβ) peptides on small
(SUV) and large unilamellar vesicles (LUVs), which consist of 1-palmitoyl-2-oleoyl-sn …

Alpha synuclein (αS) aggregates are the main component of Lewy bodies (LBs) associated
with Parkinson's disease (PD). A longstanding question about αS and PD pertains to the …