A Comprehensive Bioinformatic Assessment of Different Signal Peptides for Secretory Expression of Human Growth Hormone in Escherichia Coli: An In Silico Study

Document Type : Original Article (s)

Authors

1 MSc Student, Department of Molecular Cell Biology, School of Applied Science, University of Guilan, Rasht, Iran

2 Associate Professor, Department of Molecular Cell Biology, School of Applied Science, University of Guilan, Rasht, Iran

3 Assistant Professor, Department of Biotechnology, School of Agriculture, University of Guilan, Rasht, Iran

4 Associate Professor, Department of Biotechnology, School of Agriculture, University of Guilan, Rasht, Iran

Abstract

Background: Nowadays, by genetic engineering and bioinformatics, large scale production of pharmacological recombinant proteins in Escherichia coli (E. coli) bacteria, which has unique expression properties, becomes a routine and economic imperative. In this study, periplasmic production of human growth hormone was investigated using bioinformatics methods.Methods: The aim of this study was bioinformatic evaluation of 48 human signal peptides by reliable servers for expression analysis of human growth hormone in Escherichia coli. Accuracy and precision of 48 signal peptides were evaluated via powerful SignalP server. Physicochemical properties of remaining signal peptides were investigated using Genescript and Protparam servers. Solubility of protein, secretory activity of signal peptides after expression, and transmission mechanism of signal peptides were investigated using Solpro, ProtCompB and PRED-TAT, respectively.Findings: Theoretically, proline rich protein HaeIII subfamily 1 (PRH1), C10orf99, and prolactin-releasing hormone (PRLH) signal peptides were predicted as the most proper signal peptides in fusion of human growth hormone protein, respectively.Conclusion: Secretory expression instead of cytoplasmic expression provides benefits. This study results indicated that by examining different signal peptide sequences in fusion with human growth hormone protein, achieving signal peptides with potential and capability for high expression is possible. The accuracy of these results can be verified in future studies and experiments.

Keywords

References

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Journal of Isfahan Medical School
Volume 35, Issue 440 - Serial Number 440
May and June 2017
Pages 890-899

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History

  • Receive Date: 07 June 2017
  • Revise Date: 02 November 2024
  • Accept Date: 06 April 2022

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