Soluble Form Production of Recombinant Human Insulin-Like Growth Factor-1 by NusA Fusion Partner in E. coli
Trends in Peptide and Protein Sciences,
Vol. 4 (2019),
1 January 2019
,
Page 1-5 (e8)
https://doi.org/10.22037/tpps.v4i0.26948
Abstract
Insulin-Like Growth Factor-1 (IGF-1) is a small peptide with 70 amino acids and 7.6 kDa molecular weight that acts as the major mediator of growth hormone. According to the previous studies, recombinant production of human IGF-1 (rhIGF-1) in E. coli has resulted in an inactive form of protein (inclusion body). There are several strategies to transform inclusion body to a soluble form. Production in the form of fusion proteins as a suitable strategy, helps researcher in recombinant production of proteins in the soluble and active form. In current study, NusA fusion protein was used to produce IGF-1 soluble form, instead of insoluble protein. In previous study, rhIGF-1 was optimally expressed in inclusion body with 1.2 g/L concentration. rhIGF1 -NusA construct was cloned and expressed in E. coli, then, cell lysate was analyze by SDS-PAGE and densitometry techniques, to assay soluble and insoluble form of rhIGF-1. Results showed that rhIGF-1 concentration in soluble phase was 0.14 g/L, indicating that about 12% of total expression of rhIGF-1 was in the soluble form through NusA-fusion protein strategy. These results confirmed that some fusion proteins like NusA could improve the solubility of recombinant proteins expressed in heterogeneous bacterial hosts.
HIGHLIGHTS
- Fusion proteins is a suitable strategy for recombinant production of proteins in e soluble form.
- NusA fusion tag improves the solubility of recombinant proteins expressed in bacterial hosts.
- NusA fusion protein convert IGF-1 insoluble form to soluble form in E. coli.
- IGF-1
- NusA
- Soluble form
- Inclusion body
- E.coli
How to Cite
References
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