Water solubility and structural stability are key merits for proteins defined by the primary
sequence and 3D-conformation. Their manipulation represents important aspects of the …

Disrupted protein folding or decreased protein stability can lead to the accumulation of
(partially) un‐or misfolded proteins, which ultimately cause the formation of protein …

Intermediate species in the assembly of amyloid filaments are believed to play a central role
in neurodegenerative diseases and may constitute important targets for therapeutic …

The endoplasmic reticulum (ER) represents the entry point into the secretory pathway where
nascent proteins encounter a specialized environment for their folding and maturation …

This review is aimed to provide a concise yet extensive survey of key short bioactive peptide
sequences for a range of applications ranging from biomaterials development to peptides …

COVID-19 is primarily known as a respiratory disease caused by SARS-CoV-2. However,
neurological symptoms such as memory loss, sensory confusion, severe headaches, and …

When protein/peptides aggregate, they usually form the amyloid state consisting of cross β-
sheet structure built by repetitively stacked β-strands forming long fibrils. Amyloids are …

The phenomenon of protein aggregation and amyloid formation has become the subject of
rapidly increasing research activities across a wide range of scientific disciplines. Such …

Antimicrobial peptides (AMPs) are important components of the innate immune system that
have been found to be effective against disease causing pathogens. Identification of AMPs …

Therapeutic proteins have a propensity for aggregation during manufacturing, shipping, and
storage. The presence of aggregates in protein drug products can induce adverse immune …