Autor: |
Baseer Ahmad, Zhongxuan Li, Quratulain Hanif, Qingyong Hu, Xubiao Wei, Lulu Zhang, Shahzad Akbar Khan, Maierhaba Aihemaiti, Huma Gulzar, Muhammad Shahid, Dayong Si, Rijun Zhang |
Jazyk: |
angličtina |
Rok vydání: |
2020 |
Předmět: |
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Zdroj: |
Frontiers in Pharmacology, Vol 11 (2020) |
Druh dokumentu: |
article |
ISSN: |
1663-9812 |
DOI: |
10.3389/fphar.2020.00461 |
Popis: |
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. |
Databáze: |
Directory of Open Access Journals |
Externí odkaz: |
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