Monoclonal antibodies (mAbs) are subject to instability issues linked to their protein nature.
In this work, we review the different mechanisms that can be linked to monoclonal antibodies …

Inclusion bodies (IBs) often emerge upon overexpression of recombinant proteins in E. coli.
From IBs, refolding is necessary to generate the native protein that can be further purified to …

The secondary structure of proteins in legumes, cereals, milk products and chicken meat
was studied by diffuse reflectance infrared spectroscopy in the region of the amide I band …

Many protein species produced in recombinant bacteria aggregate as insoluble protein
clusters named inclusion bodies (IBs). IBs are discarded from further processing or are …

Bacterial inclusion bodies (IBs) have long been considered as inactive, unfolded waste
material produced by heterologous overexpression of recombinant genes. In industrial …

The prevailing current view of protein folding is the thermodynamic hypothesis, under which
the native folded conformation of a protein corresponds to the global minimum of Gibbs free …

Continuous production delivers higher productivity and better quality than traditional batch-
wise approaches. It intensifies production lowering capital cost and enables better control …

Background For a long time IBs were considered to be inactive deposits of accumulated
target proteins. In our previous studies, we discovered IBs containing a high percentage of …

The objective of the research was to understand the structural determinants governing
protein aggregation into inclusion bodies during expression of recombinant proteins in …

Protein misfolding and aggregation into amyloid structures are associated with dozens of
human diseases. Recent studies have provided compelling evidence for the existence of …