Active oligopeptides with inhibitory effect on tumor cells

An oligopeptide and anti-tumor drug technology, applied in anti-tumor drugs, peptides, drug combinations, etc., can solve the problems of increasing the survival rate of DL-tumor-bearing mice, limiting research and application, reducing the number of cells, etc., and achieves production scale The effect of large, broad application prospects and short production cycle

Inactive Publication Date: 2011-12-07
中国人民解放军63975部队
View PDF3 Cites 1 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0005] The anti-tumor effect of abrin proteolytic fragments was tested in vivo by the DL-tumor-bearing mouse model, and the results showed that ABP could significantly reduce the volume of ascites and the number of cells in the ...

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
  • Active oligopeptides with inhibitory effect on tumor cells
  • Active oligopeptides with inhibitory effect on tumor cells
  • Active oligopeptides with inhibitory effect on tumor cells

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0023] Embodiment 1, in vitro enzymatic hydrolysis and fractionation of abrin protein

[0024] 1. In vitro enzymatic hydrolysis of abrin protein

[0025] Dissolve the acacia protein sample in 20mmol / L NH 4 HCO 3 In the solution, make 2μg / μl of abrinP 2 After mixing the solution, heat at 100°C for 5min, add trypsin at a concentration of 20ng / ml to make the ratio of enzyme to substrate 1:50, and incubate at 37°C for 12h.

[0026] 2. Fractionation and separation of hydrolyzate of acacia protein

[0027] The acinia protein hydrolyzate was graded by ultrafiltration with ultrafiltration tubes with a molecular weight cut-off of 10kD and 3kD. The enzymatic hydrolysis products are divided into three groups of mixed polypeptides with molecular weight greater than 10kD and 3kD ~ 10kD and 3kD. MTT assay was used to detect the inhibitory effect of the three groups of mixed polypeptides on the proliferation of HCT-8 cells.

Embodiment 2

[0028] Example 2, Separation of Enzymolysis Mixed Polypeptides with Molecular Weight Less Than 3kD

[0029] After freeze-drying the mixed polypeptide with a molecular weight less than 3kD, it was dissolved in TFA-water containing 0.1%, filtered through a 0.22 μm filter membrane to remove the precipitate, and the enzymatically hydrolyzed mixed polypeptide was separated by RP-HPLC.

[0030] Chromatographic conditions: A phase 0.1% TFA-water, B phase 100% acetonitrile. Column temperature: 37°C; flow rate: 1ml / min; detection wavelength: 280nm. The binary elution gradient is: 0-20min, B changes from 0% to 45%; 20-55min, B changes from 45% to 100%; 55-65min, B changes from 100% to 28%; 65-80min, B went from 28% to 0%. The RP-HPLC separation products were collected in fractions with centrifuge tubes.

Embodiment 3

[0031] Example 3, Activity Identification of Mixed Polypeptide Components with Molecular Weight Less Than 3kD

[0032] After the RP-HPLC components collected in the centrifuge tube were freeze-dried, the activity of the separated components to inhibit the proliferation of HCT-8 cells was detected by the MTT method. A total of 39 fractions were collected, and the results showed that fractions 5, 26, and 28 all had the activity of inhibiting the proliferation of HCT-8.

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
Molecular weightaaaaaaaaaa
Login to view more

Abstract

The present invention discloses five kinds of active oligopeptides with inhibitory effect on tumor cells and their applications. drug. The amino acid sequences of these five oligopeptides are: 1) QAQGSNN; 2) GDLERW; 3) SLENNW; 4) GTYGDL; 5) DVTNAY. The five oligopeptides of the present invention can be obtained in large quantities by artificial synthesis, and have the advantages of short production cycle, large production scale and low production cost, so they have great practical significance and broad application in the research of tumor therapeutic drugs. Application prospect.

Description

technical field [0001] The invention relates to five kinds of active oligopeptides with inhibitory effect on tumor cells, which can be used as antitumor drugs. Background technique [0002] As early as 1969, Reddy and Sirse found that acacia extract could inhibit the growth of Yoshida sarcoma. Subsequent studies found that acacia protein had obvious curative effect on the treatment of animal leukemia and L1210 leukemia, and could significantly inhibit the proliferation of Ehrlich ascites cancer cells, It also has different degrees of antitumor activity against B16 black hemorrhoids and Lewis lung cancer. [0003] In vitro experiments have shown that abrin has significant inhibitory effects on Ehrlich ascites carcinoma, human melanoma MMX-G.E, Lewis lung cancer, and colon cancer. its limitations. [0004] In 2009, Sujit K et al put trypsin and acacia protein with a molar ratio of 1:50 in a 37°C incubator for overnight digestion, and after ultrafiltration with a filter membr...

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): C07K7/06A61K38/08A61P35/00
Inventor 鹿晓晶李丽琴石童王惠芳
Owner 中国人民解放军63975部队
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