ISSN: 0973-7510

E-ISSN: 2581-690X

Open Access
M. Rasekhian1, P. Hadadi1, F. Mirzaei2 and O. Tavallaei1
1Department of Pharmacognosy and Pharmaceutical Biotechnology, School of Pharmacy, Kermanshah University of Medical Sciences, Kermanshah, Iran.
2Student Research Committee, Kermanshah University of Medical Sciences, Kermanshah, Iran.
J Pure Appl Microbiol. 2016;10(4):2647-2653 | © The Author(s). 2016
Received: 13/06/2016 | Accepted: 19/09/2016 | Published: 31/12/2016

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.


In silico, E. coli, TRAIL, Secretion.

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© The Author(s) 2016. Open Access. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License which permits unrestricted use, sharing, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.