A Hybrid Peptide DEFB-TP5 Expressed in Methylotrophic Yeast Neutralizes LPS With Potent Anti-inflammatory Activities

• Main Authors: Baseer Ahmad (Author), Zhongxuan Li (Author), Quratulain Hanif (Author), Qingyong Hu (Author), Xubiao Wei (Author), Lulu Zhang (Author), Shahzad Akbar Khan (Author), Maierhaba Aihemaiti (Author), Huma Gulzar (Author), Muhammad Shahid (Author), Dayong Si (Author), Rijun Zhang (Author)
• Format: Book
• Published: Frontiers Media S.A., 2020-05-01T00:00:00Z.
• Subjects: article
• Online Access: Connect to this object online.

Summary

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.

Item Description

1663-9812
10.3389/fphar.2020.00461