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Investigation of Periplasmic Signal Peptides for the Expression of Thanatin Peptide in Escherichia coli
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Abbas Tanhaeian   , Leila Simaei Soltani , Seyyedeh Zahra Mousavi * |
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Abstract: (966 Views) |
Periplasmic expression of antimicrobial peptides is one of the important options in protein expression systems. In the present study, bioinformatics methods were used to predict the best signal peptide for the expression of thanatin in the host Escherichia coli. So that, the sequences of 29 signal peptides were prepared from signal peptide databases. Since the aim of this study was to introduce optimal signal peptides for periplasmic expression, the environment in which the protein functions, cleavage site, solubility, probability of secretory signal peptide and physical and chemical properties were investigated through software such as Signalp6, Psort, Protein-sol, PRED-TAT and Portparam, respectively. In the first stage, out of 29 signal peptides, 26 passed the Signalp6 filter and only 2 passed the Psort filter. The solubility and secretory properties of the signal peptides showed that only the zraP and MalE signal peptides were suitable. Finally, the physical and chemical properties of the two peptides showed that MalE showed more favorable properties. Finally, it can be concluded that MalE is the best signal peptide for the expression of thanatin. The results obtained can be used to design periplasmic expression constructs of thanatin in the Escherichia coli host. However, laboratory studies are recommended for final confirmation.
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| Keywords: Secretory peptide, Protein, Bioinformatics |
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Full-Text [PDF 704 kb]
(318 Downloads)
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Type of Study: Research |
Subject:
Special
Received: 2025/02/17 | Accepted: 2026/05/16 | Published: 2026/05/20
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