Abstract
DEFB-TP5 is a novel auspicious health-beneficial peptide derivative from two naturally occurring peptides, β-Defensin (DEFB) and thymopentin (TP5), and shows strong anti-inflammatory activity and binds to LPS without cytotoxicity and hemolytic effect. Furthermore, the application of DEFB-TP5 peptide is inadequate by its high cost. In the current study, we developed a biocompatible mechanism for expression of the DEFB-TP5 peptide in Pichia pastoris. The transgenic strain of hybrid DEFB-TP5 peptide with a molecular weight of 6.7kDa as predictable was obtained. The recombinant DEFB-TP5 peptide was purified by Ni-NTA chromatography, estimated 30.41 mg/L was obtained from the cell culture medium with 98.2% purity. Additionally, The purified DEFB-TP5 peptide significantly (p< 0.05) diminished the release of nitric oxide (NO), TNF-α, IL-6, IL-1β in LPS-stimulated RAW264.7 macrophages in a dose-dependent manner. This study will not only help to understand the molecular mechanism of expression that can potentially be used to develop an anti-endotoxin peptide but also to serve as the basis for the development of antimicrobial and anti-inflammatory agents as well, which also provides a potential source for the production of recombinant bioactive DEFB-TP5 at the industrial level.
Highlights
About 500 antipathogenic natural peptides have been revealed to show potential actions against microbes
The recombinant DEFB-TP5 gene was amplified by PCR, it was tagged with 6 × Histadine at C-terminal that facilitate the upcoming peptide purification
The DEFB-TP5 peptide was synthesized and inserted into pUC57vector after double digested with EcoR I and Not I
Summary
About 500 antipathogenic natural peptides have been revealed to show potential actions against microbes. Segregation of these peptides has been done from an extensive variety of organisms such as vertebrates, invertebrates, bacteria, plants and fungi (Hancock and Chapple, 1999; Shah et al, 2017). The limited number of antimicrobial, anti-endotoxin, immunomodulatory and antiinflammatory agents have prompted and reinforced the urgent need to search and identify new compounds. These therapeutic agents’ origin-based antimicrobial peptides work by a novel mechanism of action (Weinstein, 1998; Jones, 2001). The immunomodulatory, and anti-inflammatory properties of AMPs can be exploited to treat inflammation and sepsis (Hu et al, 2014; Martin et al, 2015; Matzneller et al, 2017)
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