Abstract
BackgroundThe current study was aimed at evaluating the role of the N-SH2 domain of SHP-2 as a partner protein in the expression of a toxic peptide, laterosporulin (LTS). We also investigated its effects on the formation of the disulfide bond and functional folding of the peptide in vitro. The N-SH2-LTS protein was expressed as a His-tagged fusion protein, capable of undergoing enzymatic cleavage.ResultsBased on the data presented herein, the total yield of the folded fusion protein from inclusion bodies was found to be about 105 mg/l, demonstrating a high-level of heterologous expression. After enzymatic cleavage, 1.5 mg of the folded recombinant laterosporulin was obtained from each 10 mg of the fusion protein. The purity of the recombinant laterosporulin was analyzed by RP-HPLC, to yield peptides with suitable purity (85%).ConclusionsOur findings indicated the advantages of using the N-SH2 domain of SHP-2 as a rapid and easy approach not only in producing easy target proteins but also in its function as a chaperone. N-SH2 domain of SHP-2 can influence on the purification of laterosporulin at reasonable yield and in a cost-effective fashion. The N-SH2 domain of SHP-2 as a protein chaperone may be potentially favorable to produce other proteins with disulfide bonds.
Highlights
The current study was aimed at evaluating the role of the N-Src homology 2 (SH2) domain of SHP-2 as a partner pro‐ tein in the expression of a toxic peptide, laterosporulin (LTS)
In 2012, a novel bacteriocin produced by Brevibacillus sp. strain GI-9 was introduced and purified to evaluate its antibacterial spectrum called laterosporulin [8]
The structure of the fusion protein after modeling did not show very significant changes in terms of solubility compared to the natural structure of laterosporulin (36.3%)
Summary
The current study was aimed at evaluating the role of the N-SH2 domain of SHP-2 as a partner pro‐ tein in the expression of a toxic peptide, laterosporulin (LTS). Bacteriocins can be a very promising alternative for antibiotics due to their remarkable potency, narrow and broad killing spectrums, The ultimate production method of these active peptides in large amounts is by recombinant production. This entails the genetic manipulation and production of recombinant plasmids encompassing genes that encode the corresponding peptides [7]. Strain GI-9 was introduced and purified to evaluate its antibacterial spectrum called laterosporulin [8] This heat‐stable peptide with 50 amino acids in length and a molecular weight of 5750 Da, is a cysteine‐ rich peptide consisting of three disulfide bonds in its structure [8]. Based on the available data, laterosporulin exhibited four β-strands forming a twisted β-sheet
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