Biomolecular assembly is a key driving force in nearly all life processes, providing structure,
information storage, and communication within cells and at the whole organism level. These …

Herein we present a comparative study of the effects of isoquinoline alkaloids belonging to
benzo [c] phenanthridine and berberine families on β-amyloid aggregation. Results …

In humans, β-amyloid and islet amyloid polypeptide (IAPP, also known as amylin)
aggregations are linked to Alzheimer's disease and type-2 diabetes, respectively. There is …

Increasing evidence suggests that amyloid polymorphism gives rise to different strains of
amyloids with distinct toxicities and pathology-spreading properties. Validating this …

Amyloid-β and α-synuclein are intrinsically disordered proteins (IDPs), which are at the
center of Alzheimer's and Parkinson's disease pathologies, respectively. These IDPs are …

In prion diseases, fibrillar assemblies of misfolded prion protein (PrP) self-propagate by
incorporating PrP monomers. These assemblies can evolve to adapt to changing …

Polymorphism in the structure of amyloid fibrils suggests the existence of many different
assembly pathways. Characterization of this heterogeneity is the key to understanding the …

Antibody‐mediated removal of aggregated β‐amyloid (Aβ) is the current, most clinically
advanced potential disease‐modifying treatment approach for Alzheimer's disease. We …

Amyloid-β (Aβ) aggregation intermediates, including oligomers and protofibrils (PFs), have
attracted attention as neurotoxic aggregates in Alzheimer's disease. However, due to the …

Quantifying physical differences of protein aggregates implicated in Alzheimer's disease
(AD), in blood, could provide crucial information on disease stages. Here, red blood cells …