Protein aggregation has been recognized as one of the major challenges in the
development and commercialization of successful protein-based drug products because of …

Stabilization and formulation of therapeutic proteins against physical instability, both
structural alterations and aggregation, is particularly challenging not only due to each …

Disulfide bonds are naturally formed in more than 50% of amyloidogenic proteins, but the
exact role of disulfide bonds in protein aggregation is still not well-understood. The …

Oligomeric intermediates on the pathway of amyloid fibrillation are suspected as the main
cytotoxins responsible for amyloid-related pathogenicity. As they appear to be a part of the …

Aβ oligomers (AβOs) are crucially involved in Alzheimer's Disease (AD). However, the lack
of selective approaches for targeting these polymorphic Aβ assemblies represents a major …

A method is designed to quickly form protein hydrogels, based on the self-assembly of
highly concentrated lysozyme solutions in acidic conditions. Their properties can be easily …

The misfolding of proteins can lead to fibrillar and non-fibrillar deposits that are the hallmark
of numerous human diseases. Inhibition of protein aggregation is considered as a promising …

Anomalous aggregation of proteins into amyloid fibrils leads to various amyloidosis
diseases including neurodegenerative disorders. Inhibition of fibrillation process and rupture …

Misfolded β-sheet-rich protein aggregates termed amyloid, deposit in vivo leading to
debilitating diseases such as Alzheimer's, prion and renal amyloidosis diseases etc …

Hfq is a bacterial protein that regulates gene expression at the post-transcriptional level in
Gram-negative bacteria. We have previously shown that Escherichia coli Hfq protein, and …