The presence of fibrillar protein deposits (amyloid) of human islet amyloid polypeptide
(hIAPP) in the pancreatic islets of Langerhans is thought to be related to death of the insulin …

Human islet amyloid polypeptide (IAPP or amylin) is a 37‐residue hormone found as fibrillar
deposits in pancreatic extracts of nearly all type II diabetics. Although the cellular toxicity of …

The nature of the “toxic gain of function” that results from amyotrophic lateral sclerosis (ALS)-
, Parkinson-, and Alzheimer-related mutations is a matter of debate. As a result no adequate …

The role of water in promoting the formation of protofilaments (the basic building blocks of
amyloid fibrils) is investigated using fully atomic molecular dynamics simulations. Our model …

Amyloids are proteinaceous fibers commonly associated with neurodegenerative diseases
and prion-based encephalopathies. Many different polypeptides can form amyloid fibers …

A terminally protected self-assembling pentapeptide Boc-Leu (1)-Val (2)-Phe (3)-Phe (4)-Ala
(5)-OMe 1 bearing sequence similarity with Aβ17–21 (the fragment 17–21 of the amyloid β …

By using a self‐assembled amyloid from lysozyme as biotemplate we produced an ultrathin
silver wire of 1 nm diameter and up to 2 μm in length, which is at the limit attainable in …

Type II diabetes mellitus is a disease which is characterized by peripheral insulin resistance
coupled with a progressive loss of insulin secretion that is associated with a decrease in …

The molecular mechanism of amyloid formation by the islet amyloid polypeptide (IAPP) has
been intensively studied since its identification in the late 1980s. The IAPP (20–29) region is …

CH–Pi stacking interactions between carbohydrates and aromatic compounds play a central
role in biomolecular recognition, especially in lectin–sugar and protein–glycolipid systems …