Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting
either the central nervous system or a variety of peripheral tissues. Structural and dynamic …

Bacterial infections occur when wound healing fails to reach the final stage of healing, which
is usually hindered by the presence of different pathogens. Different topical antimicrobial …

The aggregation of the tau protein plays a significant role in Alzheimer's disease, and the tau
R3–R4 domain spanning residues 306–378 was shown to form the amyloid fibril core of a …

Several neurodegenerative disorders arise from the abnormal protein aggregation in the
nervous tissue leading tointracellular inclusions or extracellular aggregates in specific brain …

A tau R3–R4 domain spanning residues 306–378 was shown to form an amyloid fibril core
of a full-length tau in the brain of patients with Alzheimer's disease. Recently, we studied the …

In several neurodegenerative diseases, cell toxicity can emerge from damage produced by
amyloid aggregates to lipid membranes. The details accounting for this damage are poorly …

The interactions of amyloid oligomers with membranes are known to contribute to cellular
toxicity. Numerous in vitro experimental studies reported on the insertion of oligomers of …

α-Synuclein (αS) is a presynaptic protein that binds to cell membranes and is linked to
Parkinson's disease (PD). Binding of αS to membranes is a likely first step in the molecular …

Amyloid cross-seeding of different amyloid proteins is considered as a highly possible
mechanism for exacerbating the transmissible pathogenesis of protein misfolding disease …

Amphipathic peptides can cause biological membranes to leak either by dissolving their
lipid content via a detergent-like mechanism or by forming pores on the membrane surface …