Self-assembled peptide nanostructures have been increasingly exploited as functional
materials for applications in biomedicine and energy. The emergent properties of these …

Freeze tolerance–the ability to survive internal ice formation–has evolved repeatedly in
insects, facilitating survival in environments with low temperatures and/or high risk of …

Amyloidogenic diseases are characterised by the formation of amyloid aggregates inside or
outside the cell. Amyloid-associated human diseases include Alzheimer's disease …

Most of the cell's chemical reactions and structural components are facilitated by proteins.
But proteins are highly dynamic molecules, where numerous modifications or changes in the …

Protein misfolding and aggregation have attracted immense research interests due to their
connection with an array of degenerative diseases including neurodegenerative disorders …

Introduction The most prevalent biological macromolecules in living systems are proteins,
the building block of life, extremely dynamic in structure and functions. Due to several …

Before the controversial approval of humanized monoclonal antibody lecanemab, which
binds to the soluble amyloid‐β protofibrils, all the treatments available earlier, for …

Protein misfolding and amyloid formation are hallmarks of numerous diseases, including
amyotrophic lateral sclerosis (ALS), in which hSOD1 aggregation is involved in …

Protein molecules are amphiphilic moieties that spontaneously adsorb at the air/solution
(A/S) interface to lower the surface energy. Previous studies have shown that hydrodynamic …

The presence of neuritic plaques and amyloid fibrils arising from the misfolding of certain
proteins is the principal molecular indicator of neurodegenerative diseases such as …