Periplaneta americana peptide C with anti-hepatoma activity and application of periplaneta americana peptide C

A technology of anti-liver cancer and cockroach peptide, which is applied in the field of medicine, can solve problems such as hypersensitivity, failure to meet the needs of the pharmaceutical market, and lower drug efficacy, and achieve the effect of small dosage

Active Publication Date: 2017-10-17
DALI UNIV
View PDF3 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

These extracts have a great impact on the further preparation of anticancer drugs. For example, impurities in the extracts are likely to cause hypersensitivity, which limits the way of drug use. At the same time, further separation and puri

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
  • Periplaneta americana peptide C with anti-hepatoma activity and application of periplaneta americana peptide C
  • Periplaneta americana peptide C with anti-hepatoma activity and application of periplaneta americana peptide C
  • Periplaneta americana peptide C with anti-hepatoma activity and application of periplaneta americana peptide C

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0034] American cockroach peptide C exists in the medicinal materials of Periplaneta americana. The extraction method of the American cockroach peptide C comprises the following steps: after extracting the Periplaneta americana medicinal material with a solvent, and then repeatedly extracting and separating by macroporous resin adsorption, dextran gel column chromatography, high performance liquid chromatography, etc., A sample containing peptidic acid C was obtained.

[0035] The polypeptide sequence Asp-Leu-Asn-Asn-Ser-Arg-Lys of American cockroach peptide C was entrusted to Sangon Bioengineering (Shanghai) Co., Ltd. for synthesis. The physical and chemical properties of peptide C are as follows:

[0036] Number of amino acid residues:

7

1 character:

DLNNSRK

3 characters:

Asp-Leu-Asn-Asn-Ser-Arg-Lys

Molecular weight:

845.91g / mol

Isoelectric point:

10.1

Net charge at PH=7:

1.0

Average Hydrophilicity:

...

Embodiment 2

[0041] 1. Cell culture of human liver cancer HepG2 cell line

[0042] Human liver cancer HepG2 cell line adopts high-glucose DMEM complete medium containing 10% fetal bovine serum, placed in 5% CO 2 , Cultured in a 37°C incubator, and the cells in the logarithmic growth phase were taken for experiments.

[0043] 2. MTT method to detect the survival rate of human liver cancer cell HepG2 cells after treatment

[0044] HepG2 cell seed plate (1×10 5 mL -1, 100 μL) were inoculated in a 96-well plate and cultured for 24 h. Prepare the American cockroach peptide C solutions with concentrations of 6.25, 12.5, 25, 50, 100, and 150 μg / mL, intervene with the above-mentioned 6 concentrations of Periplaneta americana peptide solutions, set 6 replicate wells for each concentration, and set up 6 replicate wells for each concentration. 200 μL, set thalidomide (concentration: 100 μg / mL, 200 μg / mL) positive control group and blank control group at the same time, continue to culture for 24 h...

Embodiment 3

[0057] Inhibition of Migration of HepG2 Cells by Peptide C in Cell Scratch Test

[0058] Experimental grouping: blank control group, thalidomide control group (concentration of 100 μg / mL, 200 μg / mL), meicockatide C concentration set to low, medium and high dose groups (25 μg / mL, 50 μg / mL, 100 μg / mL mL, 150 μg / mL).

[0059] HepG2 cells were routinely digested at a density of 2×10 5 mL -1 Inoculate in a 6-well plate, 2 mL per well. After culturing for 24 hours, use a 200 μL pipette tip to draw a straight line at the bottom of the 6-well plate, wash with PBS 2 to 3 times, and add drugs according to the experimental groups. Take pictures of the scratches at 0h and 24h respectively, and measure the width of the scratches. The above experiment was repeated three times, and the average value was taken to calculate the scratch healing rate. Scratch healing rate=(0h scratch width-24h scratch width) / 0h scratch width×100%.

[0060] SPSS 17.0 statistical software and OriginPro 8.6 g...

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

No PUM Login to view more

Abstract

The invention provides periplaneta americana peptide C with anti-hepatoma activity and application of the periplaneta americana peptide C, and belongs to the technical field of medicines. The periplaneta americana peptide C with anti-hepatoma activity has an amino acid sequence as shown in a sequence table SEQ ID No. 1. The periplaneta americana peptide C can be applied to preparation of drugs for preventing and/or treating hepatoma. The periplaneta americana peptide C can effectively inhibit cell proliferation and migration of hepatoma cells HepG2, and the inhibition strength is increased along with increasing of the concentration of the periplaneta americana peptide C. compared with another periplaneta americana extract, the periplaneta americana peptide C has obvious advantages on inhibition of HepG2 proliferation. Compared with thalidomide positive control, the periplaneta americana peptide C has the same or excellent anti-hepatoma effect. The provided periplaneta americana peptide C is polypeptide, and can be produced conveniently and economically on a large scale in an artificial synthesis mode, therefore, limitation to active substance sources is eliminated, and requirements of markets and production can be met.

Description

technical field [0001] The invention belongs to the technical field of medicine, and in particular relates to a cockroach peptide C with anti-liver cancer activity and its application. Background technique [0002] At present, due to environmental pollution and other problems brought about by industrial development, the quality of human living environment is continuously declining, and the incidence and mortality of tumor diseases are also increasing, which seriously threatens people's health and life. The occurrence of cancer is affected by many reasons, such as environmental pollution, chemical pollution, ionizing radiation, free radical toxins or microorganisms and their metabolic toxins and other carcinogens, and may also be affected by the body itself, such as genetic characteristics, endocrine imbalance, immune Functional disorders, etc. can also cause normal cells to become cancerous. According to data released by the International Union Against Cancer, cancer deaths...

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): C07K7/06A61K38/08A61P35/00A61P35/04
CPCA61K38/00C07K7/06
Inventor 刘熙高孟婷郑园园张蕊袁发璐李婷刘衡彭芳
Owner DALI 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