Amyloids can have normal biological functions. 1r3 However, amyloidogenic proteins can
also form unwanted oligomeric or polymeric aggregates when disturbed from their native …

The rational design of amyloid oligomer inhibitors is yet an unmet drug development need.
Previous studies have identified the role of tryptophan in amyloid recognition, association …

Evidence is growing at an increasing pace that amyloid fibers are not just the result of
aberrant protein folding associated with neurodegenerative diseases, but are widespread in …

Numerous short peptides have been shown to form β‐sheet amyloid aggregates in vitro.
Proteins that contain such sequences are likely to be problematic for a cell, due to their …

Purpose To analyze contribution of short aggregation-prone regions (APRs), which may self-
associate via cross-β motif and were earlier identified in therapeutic mAbs, towards antigen …

Experiments hold intriguing, circumstantial clues to the mechanisms behind arginine-
mediated solubilization of small organic drugs and suppression of protein aggregation …

Formation of toxic amyloid structures is believed to be associated with various late‐onset
neurodegenerative disorders such as Alzheimer's and Parkinson's diseases. The fact that …

Among the forces responsible for shaping proteins, interactions between side chains of
aromatic residues play an important role as they are involved in the secondary and the …

Using experimental and computational methods we identified the effects of mutation on the
structure and dynamics of the amyloidogenic peptide apoC-II (60–70), in monomeric and …

The self‐assembly of peptide YYKLVFFC based on a fragment of the amyloid beta (Aβ)
peptide, Aβ16–20, KLVFF has been studied in aqueous solution. The peptide is designed …