Application of natural host defensin Cm-CATH2

A host defense peptide, cm-cath2 technology, applied in the field of peptide applications, can solve the problems of unscientific, bacterial drug resistance and drug residues, and achieve the effect of improving resistance, broad-spectrum and high-efficiency antibacterial effect, and wide application prospects

Pending Publication Date: 2020-09-15
SUZHOU UNIV
View PDF1 Cites 3 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[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

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Application of natural host defensin Cm-CATH2
  • Application of natural host defensin Cm-CATH2
  • Application of natural host defensin Cm-CATH2

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0025] Example 1 Preparation of Cm-CATH2

[0026] (1) Using an automatic peptide synthesizer (433A, Applied Biosystems) to synthesize the complete sequence of Cm-CATH2 derived from the reptile green sea turtle, and desalting and purifying it 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 Cm-CATH2 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 Cm-CATH2 of the present invention is shown in SEQ ID No.1. It consists of 33 amin...

Embodiment 2

[0030] Example 2 Detection of Antibacterial Activity of Cm-CATH2 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 on the surface of the culture medium, drop 10 μL of 2 mg / mL Cm-CATH2 sample solution dissolved in sterilized deionized water, and incubate 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), Cm-CATH2 minimum inhibitory concentration (Minimum Inhibitory Concentration) determination (2-fold dilution method):

[0033] Select the strains wit...

Embodiment 3

[0042] Example 3 Determination of Cm-CATH2 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 Cm-CATH2 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 with the Cm-CATH2 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 respectively, and then take 50 μL of the diluted bacterial solution for coating 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. Cm-CATH2 has a rapid bactericidal speed on Vibrio ...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more

PUM

PropertyMeasurementUnit
Minimum inhibitory concentrationaaaaaaaaaa
Molecular weightaaaaaaaaaa
Login to view more

Abstract

The invention relates to an application of natural host defensin Cm-CATH2, in particular to an application of natural host defensin Cm-CATH2 to preparation of medicines for resisting aquatic product pathogenic bacteria, and an application of the natural host defensin Cm-CATH2 to preparation of an aquaculture animal immunization adjusting agent. The invention further discloses an application of thenatural host defensin Cm-CATH2 to preparation of an aquaculture animal feed. Research results that micropterus salmoides are used as experiment animals indicate that the Cm-CATH2 can kill varied common aquatic product pathogenic bacteria, can adjust the immune function of the micropterus salmoides, can improve the bacterial infection resistance of the micropterus salmoides, and can increase the motility rate of the micropterus salmoides. The Cm-CATH2 has broad application prospects in the field of aquaculture.

Description

technical field [0001] The invention relates to the field of polypeptide applications, in particular to the application of a natural host defense peptide Cm-CATH2. 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 increasing...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more

Application Information

Patent Timeline
no application Login to view more
IPC IPC(8): A61K38/17A61P31/04A61P37/02A61P29/00A23K50/80A23K20/147
CPCA61K38/1703A61P31/04A61P37/02A61P29/00A23K50/80A23K20/147
Inventor 王义鹏于海宁杨怀欣王妍欧阳建红
Owner SUZHOU UNIV
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Try Eureka
PatSnap group products