title: Disulfide bond formation and its impact on the biological activity and stability of recombinant therapeutic proteins produced by Escherichia coli expression system.
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.
authors.affiliation: Department of Chemical Engineering, University of Waterloo, Waterloo, Ontario, Canada N2L3G1. Lin.Zhang@dsm.com
authors.forename: Lin
authors.initials: L
authors.lastname: Zhang
authors.forename: C Perry
authors.initials: CP
authors.lastname: Chou
authors.forename: Murray
authors.initials: M
authors.lastname: Moo-Young
mesh_terms: D001709:Biotechnology / Q000379:methods; D004220:Disulfides / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D055550:Protein Stability; D011994:Recombinant Proteins / Q000096:biosynthesis* / Q000235:genetics
chemical_list: D004220:Disulfides; D011994:Recombinant Proteins