Effective production of human growth factors in Escherichia coli by fusing with small protein 6HFh8
نویسندگان
چکیده
Abstract Background Growth factors (GFs) are signaling proteins that affect cellular processes such as growth, proliferation, and differentiation. GFs used cosmeceuticals, exerting anti-wrinkle, anti-aging, whitening effects, also pharmaceuticals to treat wounds, growth failure, oral mucositis. However, in mammalian bacterial cells, low productivity expression inclusion bodies, respectively, of does not satisfy the consumer demand. Here, we aimed develop a system produces high yields soluble can be purified their native forms. Results We present Fh8, an 8-kDa peptide from Fasciola hepatica with N-terminal hexa-histidine (6HFh8), fusion partner for enhanced human GF production recombinant Escherichia coli . The harboring tobacco etch virus (TEV) protease cleavage site was fused N-terminus 10 GFs: acidic basic fibroblast (aFGF bFGF, respectively), epidermal factor (EGF), hormone (hGH), insulin-like 1 (IGF-1), vascular endothelial 165 (VEGF165), keratinocyte (KGF-1), placental (PGF), stem cell (SCF), tissue inhibitor metalloproteinase (TIMP-1). were expressed E. under control T7 promoter at three temperatures (25 °C, 30 37 °C). All individual proteins, except SCF TIMP-1, successfully overexpressed cytoplasmic form more than one temperature. Further, original aFGF, IGF-1, EGF, VEGF165 cleaved by TEV protease. Five-liter fed-batch fermentation approaches 6HFh8-aFGF (lacking disulfide bonds) 6HFh8-VEGF165 (a cysteine-rich protein) devised obtain target protein concentrations 9.7 g/l 3.4 g/l, respectively. two highly (> 99% purity). Furthermore, they exerted similar proliferative effects those commercial equivalents. Conclusions demonstrated 6HFh8-GF could on scale cytoplasm , subsequently maintaining biological activity. Hence, small 6HFh8 efficient mass-production various GFs.
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ژورنال
عنوان ژورنال: Microbial Cell Factories
سال: 2021
ISSN: ['1475-2859']
DOI: https://doi.org/10.1186/s12934-020-01502-1