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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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Published in: | Biotechnology advances 2011-11, Vol.29 (6), p.923-929 |
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container_title | Biotechnology advances |
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creator | Zhang, Lin Chou, C. Perry Moo-Young, Murray |
description | 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. |
doi_str_mv | 10.1016/j.biotechadv.2011.07.013 |
format | article |
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After assessing the research progress in detecting disulfide bond scrambling, strategies for preventing this phenomenon are proposed.</description><identifier>ISSN: 0734-9750</identifier><identifier>EISSN: 1873-1899</identifier><identifier>DOI: 10.1016/j.biotechadv.2011.07.013</identifier><identifier>PMID: 21824512</identifier><identifier>CODEN: BIADDD</identifier><language>eng</language><publisher>Kidlington: Elsevier Inc</publisher><subject>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. 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Perry</creatorcontrib><creatorcontrib>Moo-Young, Murray</creatorcontrib><title>Disulfide bond formation and its impact on the biological activity and stability of recombinant therapeutic proteins produced by Escherichia coli expression system</title><title>Biotechnology advances</title><addtitle>Biotechnol Adv</addtitle><description>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. 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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 |
title | Disulfide bond formation and its impact on the biological activity and stability of recombinant therapeutic proteins produced by Escherichia coli expression system |
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