Amyloids result from the aggregation of a set of diverse proteins, due to either specific
mutations or promoting intra-or extra-cellular conditions. Structurally, they are rich in …

Self-assembly of misfolded proteins into ordered fibrillar aggregates known as amyloid
results in various human diseases. However, more and more proteins, whether in human …

Protein fibrillation and oxidative damage are closely associated with the development of
many chronic diseases such as Alzheimer's disease, Parkinson's disease and transthyretin …

Amyloid self-assembly is pathologically linked to many neurodegenerative diseases,
including Alzheimer's disease (AD) and Parkinson's disease (PD). While many inhibitors …

Protein misfolding lead to pathological amyloid aggregates causing neurodegenerative
disorders. Interaction and effect of benzophenanthridine alkaloid, sanguinarine (SNR …

α-Synuclein (α-syn) aggregates into cytotoxic amyloid fibrils, which are recognized as the
defining neuropathological feature of Parkinson's disease (PD). Therefore, inhibiting α-syn …

Amyloid fibrillogenesis of proteins is known to be the root cause of a large number of
diseases like Parkinson's, Alzheimer's, and Huntington's disease, spongiform …

Interaction of two food colorant dyes, amaranth and tartrazine, with lysozyme was studied
employing multiple biophysical techniques. The dyes exhibited hypochromic changes in the …

Proteins can form amyloid fibrils that are the cause of various degenerative diseases. In this
work, we have investigated the potential of a crown ether, 18-crown-6, to arrest fibrillation in …

Highlights•Proline-/cysteine-modified silver nanoparticles (Pro-/Cys-AgNP) were
prepared.•Pro-AgNP/Cys-AgNP dose-dependently suppresses lysozyme amyloid fibril …