Canonical amyloid fibrils are composed of covalently identical polypeptide chains. Here, we
employ kinetic assays, atomic force microscopy, infrared spectroscopy, circular dichroism …

Aggregation of proteins into amyloid fibrils is driven by interactions between relatively small
amyloidogenic segments. The interplay between aggregation-prone and aggregation …

The self-assembly of abnormally folded proteins into amyloid fibrils is a hallmark of many
debilitating diseases, from Alzheimer's and Parkinson diseases to prion-related disorders …

Determining the structural origins of amyloid fibrillation is essential for understanding both
the pathology of amyloidosis and the rational design of inhibitors to prevent or reverse …

Peptides that self‐assemble into cross‐β‐sheet amyloid structures constitute promising
building blocks to construct highly ordered proteinaceous materials and nanoparticles …

A direct observation of amyloid aggregation from isolated peptides to cross-β fibrils is crucial
for understanding the nucleation-dependence process, but the corresponding macroscopic …

The formation of amyloid fibrils is associated with incurable diseases including Alzheimer's,
Parkinson's, and type 2 diabetes. Important mechanistic details of the self-assembly are …

The self-assembly of proteins and peptides into polymeric amyloid fibrils is a process that
has important implications ranging from the understanding of protein misfolding disorders to …

The amyloid fibril is a misfolded and undesirable state for proteins that has been proposed
to be a causative agent for a variety of fatal diseases known as amyloid diseases, such as …

In celebration of the many contributions to peptide chemistry from K.‐T. Wang's laboratory,
this manuscript explores the structure of the Aβ (10–35) fibril. This central segment of the Aβ …