ArticleBMC biotechnology2020
Intein-mediated recombinant expression of monomeric B22Asp desB30 insulin.
Article in BMC biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- X-ray crystallographic and hydrogen deuterium exchange studies confirm alternate kinetic models for homolog insulin monomers.PloS one · 2025Article
- Recombinant production of interleukin-1 receptor antagonist in fusion to albumin binding domain with potential affinity to human serum albumin.Research in pharmaceutical sciences · 2024Article
- Intein Based Fusion Proteins: Great Tags for the Soluble Production and Convenient Purification of Recombinant Proteins.Iranian journal of biotechnology · 2024Review
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Authors and funding
8 authors.
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Abstract
backgroundInsulin controls hyperglycemia caused by diabetes, and virtually all treatments require exogenous insulin. However, the product's extensive post-translational modifications have hindered the manufacture of recombinant insulin.
resultHere we report a novel production method for a monomeric B22Asp desB30 insulin analog (B22D desB30 insulin). Its precursor, DPIP, is fused to an N-terminal chitin-binding domain and intein self-cleavage tag. The fusion protein is expressed and purified from E. coli and immobilized on chitin resins. DPIP is then released using an optimized pH shift and converted to mature insulin via trypsin digest. The resulting product appears monomeric, > 90% pure and devoid of any exogenous enzyme.
conclusionThus, biologically active insulin analog can be efficiently produced in bacteria and potentially applicable in the treatment of human diabetes.
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