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

Abstract

Background: The fusion of the secretory signal peptide to the N-terminal of 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 to overcome the barriers of trial-and-error 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: 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. 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.