Evaluation of Different Signal Peptides for Secretory Production of Recombinant Human Interferon-gamma: Bioinformatics Approach

Background: The fusion of the secretory signal peptide to the N-terminal of a polypeptide’s amino acid sequence is an attractive technique for the secretory production of heterologous proteins. On the other hand, applying computational analysis may be beneficial in overcoming the barriers of trial-anderror approaches in detecting proper signal sequences. As the scope of this study, the most probable effective properties of 30 signal sequences for the extracellular production of recombinant human interferon-gamma (rhIFN-γ) were analysed. Methods: Online available web server, SignalP5.0, was used to predict signal peptides’ probability, most likely translocation pathways, and cleavage site location. The physicochemical features of signal peptides and rhIFN-γ were assessed by the ProtParam tool, and the solubility of protein was predicted by SOLpro. Results: Finally, 12 high probable signal peptides, including OmpC, PhoE, AnsB, and OmpA, were theoretically detected with ideal solubility probabilities and almost balanced physicochemical properties; hopes to be helpful in future experimental studies for the secretion of rhIFN-γ. Conclusion: The experimental analysis is required to validate the in silico results and focus on in-lab affecting factors such as cultivation methods and conditions.