The possible link between hIAPP accumulation and β-cell death in diabetic patients has
inspired numerous studies focusing on amyloid structures and aggregation pathways of this …

Unnatural helical peptidic foldamers have attracted considerable attention owing to their
unique folding behaviours, diverse artificial protein binding mechanisms, and promising …

Oligomers which form during amyloid fibril assembly are considered to be key contributors
towards amyloid disease. However, understanding how such intermediates form, their …

In the last decade, the field of sequence‐defined polymers and related ultraprecise,
monodisperse synthetic macromolecules has grown exponentially. In the early stage, mainly …

Islet amyloid polypeptide (aka IAPP, amylin) is a 37 amino acid hormone that has long been
associated with the progression of type II diabetes mellitus (TIIDM) disease. The endocrine …

Highlights•A range of functionally and structurally unrelated proteins form amyloid.•Toxic
intermediates remain elusive, making their targeting a significant challenge.•Design and …

Amylin,(or islet amyloid polypeptide; IAPP), a 37-amino acid peptide hormone, is released in
response to nutrients, including glucose, lipids or amino acids. Amylin is co-stored and co …

The conversion of the native random coil amyloid beta (Aβ) into amyloid fibers is thought to
be a key event in the progression of Alzheimer's disease (AD). A significant body of …

The islet amyloid polypeptide (IAPP), also known as amylin, is a hormone playing key
physiological roles. However, its aggregation and deposition in the pancreatic islets are …

Engineering of smart building molecules is key basis in designing intelligent drug delivery
systems. As an emerging sophisticated delivery system strategy, the powerful functions of …