Assessment of Prokaryotic Signal Peptides for Secretion of Tumor Necrosis Factor Related Apoptosis Inducing Ligand (TRAIL) in E. coli: An in silico Approach

Extracellular secretion of recombinant proteins in E. coli has various advantages, including proper folding and biological activity of proteins, lack of inclusion body, and simple steps of recombinant protein purification. But selection of a suitable signal peptide for secretion of recombinant proteins is performed mainly by trial and error which is a time-consuming and costly process. The aim of this study is in silico evaluation of common signal peptides to select the appropriate signal peptides for secretion of TRAIL protein in E. coli. SignalP server was used to predict the potential of a TRAIL-binding signal peptide and identify its correct cleavage by signal peptidase enzyme. The physicochemical properties of signal peptides and the solubility of TRAIL bound to the signal peptides were calculated by means of ProtParam and SOLpro, respectively. Results showed that of the 26 signal peptides studied, 18 signal peptides had this ability. Among these signal peptides, SfmC, OmpC, DsbA, and PhoA were good candidates for secretion of TRAIL in E. coli.

• Publication year

  2016

• Venue

  Journal of Pure and Applied Microbiology

• Publication date

  2016-12-31

• Fields of study

  Biology

• Identifiers
  DOI 10.22207/jpam.10.4.22
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar

• No claims are published for this paper.

• No concepts are published for this paper.

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