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 …

Protein–protein interactions involving β-sheet secondary structures have been questioned in
many fatal human diseases such as cancer, autoimmune and neurodegenerative diseases …

Aromatic cyclic β2, 3-amino acids (cβAAs), such as 2-aminobenzoic acid and 3-
aminothiophene-2-carboxylic acid, are building blocks that can induce unique folding …

2-Aminobenzoic acid and heterocyclic amino acids are aromatic homologues of β-amino
acids, but their chemical properties are quite distinct. Because of the poor nucleophilicity of …

Self-assembly of proteins into amyloid fibrils is a hallmark of various diseases, including
Alzheimer's disease (AD) and Type-2 diabetes Mellitus (T2DM). Aggregation of specific …

Misfolded and natively disordered globular proteins tend to aggregate together in an
interwoven fashion to form fibrous, proteinaceous deposits referred to as amyloid fibrils …

Nanoparticles, particularly carbon nanoparticles, have gathered significant interest in the
field of anti-aggregation research. However, due to their cytotoxicity, the exploration of …

Intra-cellular tau protein tangles and extra-cellular β-amyloid plaques are hallmarks of
Alzheimer's disease (AD), characterized by the conversion of natively unfolded monomeric …

Fibrous peptides such as amyloid fibrils have various roles in biological system, eg, as
causal factor of serious amyloidosis in human and as functional regulator of cell formation in …

Type 2 diabetes (T2D) is a common protein misfolding disease (PMD), and its pathogenesis
is considered to be tightly associated with the aggregation of the disease-causative hIAPP …