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 …

Self-assembled peptide and protein amyloid nanostructures have traditionally been
considered only as pathological aggregates implicated in human neurodegenerative …

During the last 100 years, cell signaling has evolved into a common mechanism for most
physiological processes across systems. Although the majority of cell signaling principles …

Recent research has provided an abundance of new information on membrane
biochemistry. Now more than ever, it is essential to update our current understanding of …

Background Regulatory approval for a biosimilar product is provided on the basis of its
comparability to an originator product. A thorough physicochemical and functional …

In antibody development and manufacturing, protein aggregation is a common challenge
that can lead to serious efficacy and safety issues. To mitigate this problem, it is important to …

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

The structural stability of proteins has been traditionally studied under conditions in which
the folding/unfolding reaction is reversible, since thermodynamic parameters can only be …

Monomeric and aggregated states of an IgG1 antibody were characterized under acidic
conditions as a function of solution pH (3.5–5.5). A combination of intrinsic/extrinsic …

Purpose The aim of this study was to develop a method to characterize intact soluble
monoclonal IgG1 antibody (IgG) oligomers by mass spectrometry. Methods IgG aggregates …