| 标题 |
Synthetic Intrinsically Disordered Proteins Enable Soluble Expression of Disulfide-Rich Therapeutics in E. coli |
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| DOI | |
| 其它 | We previously reported the de novo design of three small (<20 kDa), highly soluble synthetic intrinsically disordered proteins (SynIDPs) and demonstrated their utility as solubility tags for proteins and antifouling agents. Building on this work, we now show that these hypersoluble SynIDPs significantly enhance the soluble expression of disulfide-rich proteins (DRPs) of therapeutic relevance, including fibroblast growth factor 21 (FGF-21), interleukin-15 (IL-15), and bovine pancreatic trypsin inhibitor (BPTI). Through SynIDP fusions, we achieve soluble recombinant production of functionally active DRPs containing a single disulfide bond in the E. coli strain BL21(DE3) and up to three nonconsecutive disulfide bonds in the E. coli SHuffle T7 Express strain, without the need for refolding. |
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(2025-6-4)