Alzheimer's disease (AD) challenges our society with an annual estimated cost of $1.08
trillion in the United States alone by 2050. 1 AD is a progressive irreversible neurological …

Protein aggregation is a topic of immense interest to the scientific community due to its role
in several neurodegenerative diseases/disorders and industrial importance. Several in silico …

Amyloid fibril deposits of the intrinsically disordered hIAPP peptide are found in 95% of type
II diabetes patients, and the aggregation of this peptide is suggested to induce apoptotic cell …

Bacterial trapping using nanonets is a ubiquitous immune defense mechanism against
infectious microbes. These nanonets can entrap microbial cells, effectively arresting their …

Protein aggregation into highly structured amyloid fibrils is associated with various diseases
including Alzheimer's disease, Parkinson's disease, and type II diabetes. Amyloids can also …

A critical step of β-amyloid fibril formation is fibril elongation in which amyloid-β monomers
undergo structural transitions to fibrillar structures upon their binding to fibril tips. The atomic …

In order to evaluate potential therapeutic targets for treatment of amyloidoses such as
Alzheimer's disease (AD), it is essential to determine the structures of toxic amyloid …

Molecular self-assembly is pivotal for the formation of ordered nanostructures, yet the
structural diversity obtained by the use of a single type of building block is limited …

This Perspective highlights recent computational approaches to protein aggregation, from
coarse-grained models to atomistic simulations, using the islet amyloid polypeptide (IAPP) …

Amyloid β (Aβ) protein is responsible for Alzheimer's disease, and one of its important
fragments, Aβ (25–35), is found in the brain and has been shown to be neurotoxic …