Disulfide bond formation and its impact on the biological activity and stability of recombinant therapeutic proteins produced by Escherichia coli expression system

Therapeutic proteins require correct disulfide bond formation for biological activity and stability. This makes their manufacturing and storage inherently challenging since disulfide bonds can be aberrantly formed and/or undergo significant structural changes. In this paper the mechanisms of disulfi...

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Bibliographic Details
Published in:Biotechnology advances 2011-11, Vol.29 (6), p.923-929
Main Authors: Zhang, Lin, Chou, C. Perry, Moo-Young, Murray
Format: Article
Language:English
Subjects:
bioactive properties
Biological activity
Biological and medical sciences
biopharmaceuticals
Biotechnology
Biotechnology - methods
Disulfide bond formation/scrambling
disulfide bonds
Disulfides - metabolism
Escherichia coli
Escherichia coli - genetics
Escherichia coli - metabolism
Fundamental and applied biological sciences. Psychology
manufacturing
Protein Stability
recombinant proteins
Recombinant Proteins - biosynthesis
Recombinant Proteins - genetics
Recombinant therapeutic protein
Stability
storage quality
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Summary:Therapeutic proteins require correct disulfide bond formation for biological activity and stability. This makes their manufacturing and storage inherently challenging since disulfide bonds can be aberrantly formed and/or undergo significant structural changes. In this paper the mechanisms of disulfide bond formation and scrambling are reviewed, with a focus on their impact on the biological activity and storage stability of recombinant proteins. After assessing the research progress in detecting disulfide bond scrambling, strategies for preventing this phenomenon are proposed.
ISSN:0734-9750
1873-1899
DOI:10.1016/j.biotechadv.2011.07.013