In Silico Selection of an Optimal Signal Peptide for Improve Expression and Secretion of Human Interferon Alpha ۲b (IFN-۲b) in E. coli

Escherichia coli is the most commonly used host for the expression of recombinant proteins. However, cytoplasmic expression is the main challenges in the production of recombinant proteins in E. coli, due to formation of insoluble aggregates known as inclusion bodies. To prevent the formation of inclusion bodies, several strategies such as the use of E. coli strains with oxidative cytoplasmic environment, co-expression of chaperones and secretion of proteins into the periplasm or culture medium have been developed. Periplasmic expression offers several advantages over intracellular production such as a more oxidative environment for effective protein folding and strait forward downstream purification process without cell lysis. The N-terminal signal peptide is highly essential for secretion of recombinant proteins into the periplasm. Therefore, one of the strategies to improve the secretion efficiency is the optimization of signal peptide. Selection of an optimal signal sequence is the first important step in constructing an extracellular recombinant protein secretion system. However, there is no universal rule for selecting an appropriate signal peptide for the secretion efficiency. The nucleotide sequence encoding the signal peptide also influence ۵′mRNA secondary structure, which is an important factor in translation efficiency. In this study, we evaluated different signal peptides and theoretically determine appropriate ones for improved expression and secretion of interferon alpha ۲b (IFN-۲b) in the E. coli.

کلیدواژه ها:

Signal Peptide ، interferon alpha ۲b ، in silico ، Secretory Expression ، E. coli