Refolding techniques for recovering biologically active recombinant proteins from inclusion bodies

H Yamaguchi, M Miyazaki - Biomolecules, 2014 - mdpi.com
Biologically active proteins are useful for studying the biological functions of genes and for
the development of therapeutic drugs and biomaterials in a biotechnology industry …

Role of arginine in protein refolding, solubilization, and purification

K Tsumoto, M Umetsu, I Kumagai, D Ejima… - Biotechnology …, 2004 - Wiley Online Library
Recombinant proteins are often expressed in the form of insoluble inclusion bodies in
bacteria. To facilitate refolding of recombinant proteins obtained from inclusion bodies, 0.1 to …

[HTML][HTML] Stapled peptides inhibitors: a new window for target drug discovery

AM Ali, J Atmaj, N Van Oosterwijk, MR Groves… - Computational and …, 2019 - Elsevier
Protein-protein interaction (PPI) is a hot topic in clinical research as protein networking has a
major impact in human disease. Such PPIs are potential drugs targets, leading to the need …

The effects of arginine on refolding of aggregated proteins: not facilitate refolding, but suppress aggregation

T Arakawa, K Tsumoto - Biochemical and biophysical research …, 2003 - Elsevier
Arginine is one of the universal reagents that are effective in assisting refolding of
recombinant proteins from inclusion bodies. The mechanism of the effects of arginine on …

Effect of additives on protein aggregation

H Hamada, T Arakawa, K Shiraki - Current pharmaceutical …, 2009 - ingentaconnect.com
This paper overviews solution additives that affect protein stability and aggregation during
refolding, heating, and freezing processes. Solution additives are mainly grouped into two …

How additives influence the refolding of immunoglobulin-folded proteins in a stepwise dialysis system: Spectroscopic evidence for highly efficient refolding of a single …

M Umetsu, K Tsumoto, M Hara, K Ashish… - Journal of Biological …, 2003 - ASBMB
The gradual removal of the denaturing reagent guanidine HCl (GdnHCl) using stepwise
dialysis with the introduction of an oxidizing reagent and l-arginine resulted in the highly …

l‐Arginine increases the solubility of unfolded species of hen egg white lysozyme

RC Reddy K, H Lilie, R Rudolph, C Lange - Protein Science, 2005 - Wiley Online Library
Abstract l‐Arginine (l‐Arg) has been widely used as an enhancer of protein renaturation.
The mechanism behind its action is still not fully understood. Using hen egg white lysozyme …

An open-label, two-arm, phase I trial of recombinant human interleukin-21 in patients with metastatic melanoma

ID Davis, BK Skrumsager, J Cebon, T Nicholaou… - Clinical Cancer …, 2007 - AACR
Abstract Purpose: Human interleukin-21 (IL-21) is a pleiotropic class I cytokine that activates
CD8+ T cells and natural killer cells. We report a phase 1 study of recombinant human IL-21 …

Swee** away protein aggregation with entropic bristles: intrinsically disordered protein fusions enhance soluble expression

AA Santner, CH Croy, FH Vasanwala, VN Uversky… - Biochemistry, 2012 - ACS Publications
Intrinsically disordered, highly charged protein sequences act as entropic bristles (EBs),
which, when translationally fused to partner proteins, serve as effective solubilizers by …

Suppression of protein aggregation by L-arginine

C Lange, R Rudolph - Current pharmaceutical biotechnology, 2009 - ingentaconnect.com
L-Arginine is one of the most commonly used and most generally applicable suppressors of
protein aggregation. Its effect as enhancer of in vitro protein refolding was serendipitously …