| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10231681 | Biotechnology Advances | 2011 | 7 Pages |
Abstract
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.
Keywords
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Bioengineering
Authors
Lin Zhang, C. Perry Chou, Murray Moo-Young,