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Efficient protein production inspired by how spiders make silk
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2017 (English)In: Nature Communications, ISSN 2041-1723, E-ISSN 2041-1723, Vol. 8, 15504Article in journal (Refereed) Published
Abstract [en]

Membrane proteins are targets of most available pharmaceuticals, but they are difficult to produce recombinantly, like many other aggregation-prone proteins. Spiders can produce silk proteins at huge concentrations by sequestering their aggregation-prone regions in micellar structures, where the very soluble N-terminal domain (NT) forms the shell. We hypothesize that fusion to NT could similarly solubilize non-spidroin proteins, and design a charge-reversed mutant (NT star) that is pH insensitive, stabilized and hypersoluble compared to wildtype NT. NT star-transmembrane protein fusions yield up to eight times more of soluble protein in Escherichia coli than fusions with several conventional tags. NT star enables transmembrane peptide purification to homogeneity without chromatography and manufacture of low-cost synthetic lung surfactant that works in an animal model of respiratory disease. NT star also allows efficient expression and purification of non-transmembrane proteins, which are otherwise refractory to recombinant production, and offers a new tool for reluctant proteins in general.

Place, publisher, year, edition, pages
Nature Publishing Group, 2017. Vol. 8, 15504
National Category
Biochemistry and Molecular Biology
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URN: urn:nbn:se:kth:diva-208803DOI: 10.1038/ncomms15504ISI: 000401849500001PubMedID: 28534479Scopus ID: 2-s2.0-85019934465OAI: oai:DiVA.org:kth-208803DiVA: diva2:1110065
Funder
VINNOVASwedish Research CouncilSwedish Research Council Formas
Note

QC 20170615

Available from: 2017-06-15 Created: 2017-06-15 Last updated: 2017-06-15Bibliographically approved

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