Looking for breakthrough ideas for innovation challenges? Try Patsnap Eureka!

Application of polypeptide c2orf40mpf in the preparation of antitumor drugs

A technology of C2ORF40MPF and drugs, applied in the field of biomedicine, can solve the problems of different therapeutic targets and mechanisms of action, and achieve the effect of inhibiting proliferation

Active Publication Date: 2020-01-24
SHANDONG UNIV
View PDF3 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, due to the different pathogenesis, therapeutic targets and mechanism of action of different types of tumors, there is no report about the polypeptide C2ORF40MPF in the treatment of breast cancer and lung cancer.

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 polypeptide c2orf40mpf in the preparation of antitumor drugs
  • Application of polypeptide c2orf40mpf in the preparation of antitumor drugs
  • Application of polypeptide c2orf40mpf in the preparation of antitumor drugs

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0037] Example 1: Synthesis of polypeptide C2ORF40MPF

[0038] The amino acid sequence of the polypeptide C2ORF40MPF of the present invention is: Ser-Pro-Tyr-Gly-Phe-Arg-His-Gly-Ala-Ser-Val-Asn-Tyr-Asp-Asp-Tyr (SEQ ID NO. 1), commissioned Synpeptide company conducts peptide synthesis.

[0039] In order to compare the actual effect of the tumor suppressor polypeptide C2ORF40MPF designed in the present invention, we scrambled its amino acid sequence and commissioned a company to synthesize it to obtain Scrambled C2ORF40 mimic peptide (ScrC2ORF40), whose sequence is Asp-Ala-Phe-Tyr-Tyr- Arg-Asn-Gly-Asp-His-Tyr-Pro-Val-Ser-Gly-Ser.

Embodiment 2

[0040] Example 2: MTT experiment

[0041] 1. Experimental method:

[0042] at 37°C, 5% CO 2 Breast cancer cell lines BT549, MDAMB231, and lung cancer cell lines A549, H1299 were cultured in a cell incubator with saturated humidity. When the cell density reached about 70%, the cells were washed once with PBS, digested with trypsin, and then added to the culture medium to suspend the cells and centrifuged. Collect the cells, remove the supernatant, add the culture medium to resuspend the cells and count the cells. 3 The density per well was inoculated into 96-well plates; after culturing for 24 hours, the medium was replaced, and the medium containing different doses of polypeptides (polypeptides C2ORF40MPF and ScrC2ORF40 prepared in Example 1) were added respectively, and the culture was continued; Add 10 μl of 5 mg / ml MTT solution to each well, continue to incubate for 4 h to remove the supernatant from each well, then add 150 μl of DMSO solution, place it on a shaker and sh...

Embodiment 3

[0048] Example 3: Clone formation experiments

[0049] 1. Experimental method

[0050] BT549 and MDAMB231 cells were inoculated into 6cm dishes, 500 cells / dish, and the medium was replaced after culturing for 96 hours, and the culture medium containing 100 μM ScrC2ORF40 or 100 μM C2ORF40MPF polypeptide was added, and the culture was continued for about 2 weeks, and the culture was terminated. The culture medium was discarded, washed twice with PBS, and 5 ml of methanol was added to fix the cells. After 15 minutes, the fixative was removed, and 1 ml of Giemsa was added to stain for 30 minutes. Then, gently wash off the dye solution with running water, dry the petri dish in the air, and finally count the number of clones under the microscope, according to the number of cells per clone: ​​30-50, 50-100, 100-200, >200 The number of clones was counted separately.

[0051] 2. Experimental results:

[0052] The experimental results are as figure 2 As shown, in the figure, A and ...

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 discloses application of polypeptide C2ORF40MPF in preparing antitumor drugs. The polypeptide C2ORF40MPF has amino acid sequence as shown in SEQ ID No.1. According to the invention, the biological functions of the polypeptide C2ORF40MPF in tumor cell multiplication, migration, invasion, tumor formation, and so on are studies. In vitro experiments indicate that C2ORF40MPF can remarkably inhibit breast cancer and lung cancer cell multiplication capacity, and has remarkable inhibitory action on tumor cell migration and invasion. Meanwhile, in vivo experiments indicate that C2ORF40MPF can remarkably inhibit tumor growth in a nude mice allografted tumor model. More importantly, cell cycle experiments indicate that the polypeptide can exert the antitumor effect by inducing mitotic period retardation.

Description

technical field [0001] The invention relates to the technical field of biomedicine, in particular to the application of polypeptide C2ORF40MPF in the preparation of antitumor drugs. Background technique [0002] In China, more than 1.6 million people are diagnosed with cancer every year, and about 1.2 million people die from cancer. Since the 1990s, breast cancer rates in China have grown at more than twice the global rate, particularly in urban areas. At present, breast cancer is the tumor with the highest incidence rate in Chinese women, and its mortality rate ranks sixth among tumor malignancies. It has become a major disease that endangers human health. Therefore, it is of great significance to strengthen the research on the treatment of breast cancer and explore new therapeutic targets. [0003] Lung cancer can be divided into small cell lung cancer and non-small cell lung cancer. It is one of the malignant tumors with the highest morbidity and mortality in the world....

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
Patent Type & Authority Patents(China)
IPC IPC(8): A61K38/10A61P35/00
CPCA61K38/10
Inventor 魏光伟毛建华李超阳
Owner SHANDONG UNIV
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Patsnap Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Patsnap Eureka Blog
Learn More
PatSnap group products

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic, Popular Technical Reports.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap|About US| Contact US: help@patsnap.com