Supercharge Your Innovation With Domain-Expert AI Agents!

Application of polypeptide fl15 in the preparation of antitumor drugs

An anti-tumor drug and drug technology, applied in anti-tumor drugs, drug combinations, pharmaceutical formulations, etc., can solve the problems of poor targeting, short half-life, strong toxicity, etc., and achieve good inhibition and killing effects, convenient synthesis and safety. high effect

Active Publication Date: 2021-03-30
遵义医科大学珠海校区
View PDF3 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Of course, not all ACPs can be studied as anticancer drugs. Most ACPs have the following disadvantages, such as short half-life, easy to be hydrolyzed by protease, strong toxicity, poor targeting, etc., which cannot meet the requirements of ideal anticancer drugs. Oncopeptide Requirements

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 fl15 in the preparation of antitumor drugs
  • Application of polypeptide fl15 in the preparation of antitumor drugs
  • Application of polypeptide fl15 in the preparation of antitumor drugs

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0028] A polypeptide FL15, the amino acid sequence of which is: FLKRLFRKIRKLIRK, can be applied to the preparation of antitumor drugs.

Embodiment 2

[0029] Example 2: MTT assay detects the effect of FL15 on the proliferation of tumor cells and normal cells

[0030] Cell recovery: Take out the cryopreservation tubes of HCT-8, SKVO3, MCF-7 and HK2 cell lines from the liquid nitrogen tank, and place them in a 37°C water bath until they melt. Aspirate the thawed cell lines into 15mL sterile centrifuge tubes in a sterile ultra-clean bench, centrifuge at 1000r / min for 5min, remove the supernatant; add 5mL of fresh RPMI-1640 to HCT-8 and MCF Medium; add DMEM / F12 (1:1) complete medium to HK2. Finally transferred to the size of 25cm 2 sterile culture flask in 5% CO 2 , Cultured at 37°C.

[0031] Cell passage: observe the cells with a microscope, and the cell morphology is normal, and the cell passage is carried out when the growth density reaches about 90%. First, take out the culture bottle containing the cells and put it into the ultra-clean bench, suck out the original medium, wash the cells twice with PBS buffer, add 600 μL...

Embodiment 3

[0040] Example 3: Effect of FL15 on apoptosis of HCT-8 cells

[0041] Taking HCT-8, which has the highest therapeutic index of FL15 on tumor cells in Example 2, as an example, the effect of polypeptide FL15 on apoptosis of HCT-8 cells was explored.

[0042] Collect the HCT-8 cells in the logarithmic growth phase, prepare the cell suspension at 5×10 per well 5 Add cells to a 6-well plate at 37°C, 5% CO 2 Cultivate in the incubator for 24h.

[0043] The original medium was discarded, and FL15 drug solution prepared with fresh basal medium was added at concentrations of 0 μM (Control group, ie blank control group), 1 μM, 2 μM, and 4 μM, at 37 ° C, 5% CO 2Continue culturing for 24 h in the incubator.

[0044] After 24 hours of drug action, collect the wells and culture them in a centrifuge tube, then add 200 μL of EDTA-free trypsin to each well to digest the adherent cells, gently blow the cells with fresh medium and transfer them to a sterile centrifuge tube, 1000r / min Centri...

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
hydrophilicityaaaaaaaaaa
fluorescenceaaaaaaaaaa
Login to View More

Abstract

The invention belongs to the field of polypeptide drugs, and discloses an application of polypeptide FL15 in preparation of antitumor drugs. An amino acid sequence of the polypeptide FL15 is FLKRLFRKIRKLIRK. The anti-tumor drugs are drugs which promote apoptosis of tumor cells. The polypeptide FL15 disclosed by the invention is low in toxicity to normal cells and high in safety; and the polypeptide FL15has good inhibition and killing effects on various tumor cells of the colorectal cancer, the ovarian cancer and the breast cancer.

Description

technical field [0001] The invention belongs to the field of polypeptide drugs, in particular to the application of polypeptide FL15 in the preparation of antitumor drugs. Background technique [0002] Anticancer peptides (ACPs) are a series of peptide chains consisting of 10–60 amino acids, and their amphiphilic structure usually consists of a cationic face and a hydrophobic face, which is necessary to facilitate the interaction of the peptide with target cells. ACPs can inhibit the proliferation or migration of tumor cells, or inhibit the formation of tumor thrombus, and at the same time, it is not easy to cause drug resistance of tumor cells. The above advantages make ACPs the most promising anticancer drug candidates. Compared with general anticancer drugs, ACPs not only have more efficient antitumor activity, but also have lower toxic and side effects on normal cells, and are less likely to develop drug resistance. Of course, not all ACPs can be studied as anticancer d...

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
CPCA61K38/10A61P35/00
Inventor 杨愈丰谢明峰刘迪嘉夏前英
Owner 遵义医科大学珠海校区
Features
  • R&D
  • Intellectual Property
  • Life Sciences
  • Materials
  • Tech Scout
Why Patsnap Eureka
  • Unparalleled Data Quality
  • Higher Quality Content
  • 60% Fewer Hallucinations
Social media
Patsnap Eureka Blog
Learn More

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

© 2025 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap|About US| Contact US: help@patsnap.com