Design, expression, and characterization of the hybrid antimicrobial peptide T‐catesbeianin‐1 based on FyuA

Xu, Huihui; Tie, Kunyuan; Zhang, Yang; Feng, Xin; Cao, Yuan; Wang, Han

doi:10.1002/psc.3059

Cited by 8 publications

(6 citation statements)

References 35 publications

(56 reference statements)

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“…As expected, the target peptide DEFB-TP5 6.7 kDa was detected on SDS-page and its concentration was 30.41 mg/L. The peptide yield is greater than earlier described such as T-catesbeianin-1 (Xu et al, 2018), ceropinAD (Jin et al, 2009), and CA-MA (Xu et al, 2007).…”

Section: Discussionsupporting

confidence: 78%

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

Ahmad

Hanif

et al. 2020

Front. Pharmacol.

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DEFB-TP5 is a novel auspicious health-beneficial peptide derivative from two naturally occurring peptides, b-Defensin (DEFB) and thymopentin (TP5), and shows strong antiinflammatory 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-a, IL-6, IL-1b 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.

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Section: Discussionsupporting

confidence: 78%

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

Ahmad

Hanif

et al. 2020

Front. Pharmacol.

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“…Furthermore, the conserved amino acid sequence of the peptides have great impact on the above stated activities and also the proper replacement of some conserved sequence does not affect its activity but some suitable substitutions could improve the response of hybrid peptides (58). Hybridizing dissimilar parental peptides is an effective method to enhance the antibacterial and anti-inflammatory activities with minimum adverse effects (31, 59) such as cecropin, cathelicidin, magainin II, LL-37, and melititin (41, 60, 61).…”

Section: Discussionmentioning

confidence: 99%

Expression and Purification of Hybrid LL-37Tα1 Peptide in Pichia pastoris and Evaluation of Its Immunomodulatory and Anti-inflammatory Activities by LPS Neutralization

et al. 2019

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This study pertains to the new approach for the development of hybrid peptide LL-37Tα1 and its biomedical applications. A linear cationic hybrid peptide, LL-37Tα1 was derived from two parental peptides (LL-37 and Tα1) recognized as potent anti-endotoxin without any hemolytic or cytotoxic activity. We successfully cloned the gene of hybrid peptide LL-37Tα1 in PpICZαA vector and expressed in the Pichia pastoris . The recombinant peptide was purified by Ni-affinity column and reverse-phase high performance liquid chromatography (RP-HPLC) with an estimated molecular mass of 3.9 kDa as determined by SDS-PAGE and mass spectrometry. We analyzed the LPS neutralization by limulus amebocyte lysate (LAL) activity and the results indicate that the hybrid peptide LL-37Tα1 directly binds endotoxin and significantly ( p < 0.05) neutralizes the effect of LPS in a dose-dependent manner. Lactate dehydrogenase (LDH) assay revealed that LL-37Tα1 successfully reduces the LPS-induced cytotoxicity in mouse RAW264.7 macrophages. Moreover, it significantly ( p < 0.05) decreased the levels of nitric oxide, proinflammatory cytokines including TNF-α, IL-6, IL-1β, and diminished the number of apoptotic cells in LPS-stimulated mouse RAW264.7 macrophages. Our results suggest that the P. pastoris expression system is cost-effective for commercial production of the immunomodulatory and anti-inflammatory hybrid peptide (IAHP) LL-37Tα1 and the peptide may serve as effective anti-endotoxin/anti-inflammatory agent with minimal cytotoxicity.

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“…pestis and K. pneumoniae, as evidenced by their recognition of both FeYbt and pesticin in the two organisms. − Furthermore, an engineered hybrid toxin that contains the receptor binding domain of pesticin, and the N-terminus of T4 lysozyme, that degrades peptidoglycan (PG), killed both Y. pestis and pathogenic E.…”

Section: Ferric Siderophore Transport By Lgp Of Bacterial Pathogensmentioning

confidence: 99%

Iron Acquisition Systems of Gram-negative Bacterial Pathogens Define TonB-Dependent Pathways to Novel Antibiotics

et al. 2021

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Iron is an indispensable metabolic cofactor in both pro-and eukaryotes, which engenders a natural competition for the metal between bacterial pathogens and their human or animal hosts. Bacteria secrete siderophores that extract Fe 3+ from tissues, fluids, cells, and proteins; the ligand gated porins of the Gram-negative bacterial outer membrane actively acquire the resulting ferric siderophores, as well as other iron-containing molecules like heme. Conversely, eukaryotic hosts combat bacterial iron scavenging by sequestering Fe 3+ in binding proteins and ferritin. The variety of iron uptake systems in Gram-negative bacterial pathogens illustrates a range of chemical and biochemical mechanisms that facilitate microbial pathogenesis. This document attempts to summarize and understand these processes, to guide discovery of immunological or chemical interventions that may thwart infectious disease.

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Design, expression, and characterization of the hybrid antimicrobial peptide T‐catesbeianin‐1 based on FyuA

Cited by 8 publications

References 35 publications

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

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

Expression and Purification of Hybrid LL-37Tα1 Peptide in Pichia pastoris and Evaluation of Its Immunomodulatory and Anti-inflammatory Activities by LPS Neutralization

Iron Acquisition Systems of Gram-negative Bacterial Pathogens Define TonB-Dependent Pathways to Novel Antibiotics

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