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Application of natural host defense peptide Hc-CATH

A host defense peptide, a natural technology, applied in the field of peptide application, can solve the problem that the antibacterial activity cannot be generalized, and achieve the effect of broad-spectrum high-efficiency antibacterial effect, wide application prospect, and rapid bactericidal effect.

Pending Publication Date: 2020-09-15
SUZHOU UNIV
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0004] CN103665111A discloses the modified body of Qinghuan sea snake antibacterial peptide Hc-CATH and its preparation method and application. It has the antibacterial activity of Gram-negative bacteria and Gram-positive bacteria, but the antibacterial activity of the same polypeptide on different bacterial strains cannot be generalized. The use of developing Hc-CATH in other fields can give full play to the value of this polypeptide

Method used

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  • Application of natural host defense peptide Hc-CATH
  • Application of natural host defense peptide Hc-CATH
  • Application of natural host defense peptide Hc-CATH

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0025] Example 1 Preparation of Hc-CATH

[0026] (1) Using an automatic peptide synthesizer (433A, Applied Biosystems) to synthesize the complete sequence of Hc-CATH derived from reptiles, and desalting and purifying by HPLC reverse-phase column chromatography.

[0027] (2) The molecular weight was determined by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF).

[0028] (3) The purity of the purified Hc-CATH is identified by high performance liquid chromatography (HPLC), the molecular weight is determined by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF), the isoelectric point is determined by isoelectric focusing electrophoresis, and automatic amino acid sequencing is used Determination of amino acid sequence structure.

[0029] The amino acid sequence of the natural host defense peptide Hc-CATH of the present invention is shown in SEQ ID No.1. It consists of 30 amino acids, with a molecular w...

Embodiment 2

[0030] Example 2 Detection of Antibacterial Activity of Hc-CATH on Common Aquatic Pathogenic Bacteria

[0031] (1), respectively pick the test strains (aquatic pathogenic bacteria) preserved on the slant and smear them evenly on the nutrient broth solid medium (nutrient broth medium, British OXOID company) flat plate, the 0.5cm diameter through sterilization Place the filter paper piece on the surface of the culture medium, add dropwise 10 μL of 2 mg / mL Hc-CATH sample solution dissolved in sterilized deionized water, incubate upside down at 37°C for 18-20 hours, and observe whether the inhibition zone is formed or not. If the sample has antibacterial activity, a clear and transparent bacteriostatic zone will be formed around the filter paper, and the larger the bacteriostatic zone, the stronger the antibacterial activity of the sample.

[0032] (2), Hc-CATH minimum inhibitory concentration (Minimum Inhibitory Concentration) determination (2-fold dilution method):

[0033] Sel...

Embodiment 3

[0042] Example 3 Determination of Hc-CATH sterilization speed

[0043] Vibrio parahaemolyticus was cultured at 37°C for 12 hours with NB liquid medium (OXOID, UK), and then diluted to 10 with fresh NB liquid medium. 6 CFU / mL bacterial suspension. The Hc-CATH sample dissolved in sterilized deionized water was added to the bacterial suspension so that the final concentration was 5×MIC. Place the bacterial solution added to the Hc-CATH sample in a 37°C incubator for shaking culture, take 50 μL of the bacterial solution to dilute 1000 times at 0, 15, 30, 60, 120 and 180 minutes, and then take 50 μL of the diluted bacterial solution to spread On the NB solid medium plate, count the colonies after culturing overnight in a 37°C incubator. In this experiment, neomycin sulfate was used as a positive control, and sterilized deionized water was used as a negative control.

[0044] The results are shown in Table 3. Hc-CATH has a rapid sterilizing speed on Vibrio parahaemolyticus, and c...

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Abstract

The invention relates to application of a natural host defense peptide Hc-CATH, in particular to application of the natural host defense peptide Hc-CATH in preparation of a medicine resisting aquaticpathogenic bacteria and application in the preparation of an aquaculture animal immunomodulator. The invention further discloses application of the natural host defense peptide Hc-CATH in preparationof aquaculture animal feed. The research results using largemouth bass as experimental animals show that the Hc-CATH can kill a variety of common aquatic pathogens, regulate the immune function of largemouth bass, improve the resistance of largemouth bass to bacterial infections, and improve the survival rate of the largemouth bass. The Hc-CATH has wide application prospects in the field of aquaculture.

Description

technical field [0001] The invention relates to the application field of polypeptides, in particular to the application of a natural host defense peptide Hc-CATH. Background technique [0002] Antibiotics are chemicals produced by microorganisms that, at low concentrations, inhibit or kill other microorganisms. Antibiotics have played an important role in the development of aquaculture because of their functions of promoting animal growth, improving feed utilization, and preventing and treating animal diseases. [0003] However, with the extensive use of antibiotics in the aquaculture industry, especially the unscientific abuse, problems such as bacterial resistance and drug residues have become increasingly prominent. Due to problems such as excessive antibiotic residues, the export volume of my country's aquaculture products only accounts for 0.9%-1.2% of production, which seriously affects the development of my country's aquaculture economy. Therefore, it is increasingl...

Claims

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Application Information

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IPC IPC(8): A61K38/17A61P31/04A61P37/02A61K35/583A23K50/80A23K20/147A01K61/13
CPCA61K38/1767A61P31/04A61P37/02A61K35/583A23K50/80A23K20/147A01K61/13Y02A40/81
Inventor 王义鹏章铭辉欧阳建红张登登陈燕
Owner SUZHOU UNIV
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