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

Peptide for treatment of vascellum generation and uses thereof

一种血管、生成性的技术,应用在小肽及其应用领域,能够解决活性低、弱免疫原性、合成不方便等问题

Active Publication Date: 2008-04-02
BEIJING SAISHENG PHARMA
View PDF0 Cites 9 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0004] However, the above-mentioned endogenous anti-angiogenic proteins, because of their large molecular weight, low activity, and inconvenient synthesis, have weak immunogenicity in the preparations obtained through purification, and long-term administration can cause drug-resistant reactions

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
  • Peptide for treatment of vascellum generation and uses thereof
  • Peptide for treatment of vascellum generation and uses thereof
  • Peptide for treatment of vascellum generation and uses thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0065] The determination of embodiment 1.FpAT sequence

[0066] Using Surface-Enhanced Laser Desorption / Ionization-Time-of-Flight Mass Spectrometry (SELDI-TOF-MS) technology, gastric cancer patients (127 cases) and paired normal subjects (100 cases ) serum was analyzed to obtain serum protein expression mass spectrograms of gastric cancer and non-gastric cancer. Through model analysis based on artificial neural network, three low-molecular-weight differential proteins that can effectively distinguish gastric cancer and normal serum were screened out. When the differential protein is used as a group of gastric cancer-specific markers to diagnose gastric cancer, the sensitivity and specificity in the model group were 95.6% and 92.0%, and the accuracy rate was 93.7%; in the blind screening group, the sensitivity and specificity were 85.3% and 88%, the accuracy rate is 86.4%. Among them, a low-molecular-weight differential protein is specifically present in the serum of patients ...

Embodiment 2

[0071] Example 2. Chemical synthesis of FpAT small peptides and truncated small peptides (see Table 2 for each specific sequence)

[0072] FpAT small peptide (H 2 Chemical synthesis of N-Asp-Ser-Gly-Glu-Gly-Asp-Phe-Leu-Ala-Glu-Gly-Gly-Gly-Val-Arg-COOH):

[0073] Put the peptide synthesis column packed with 4-(2',4'-dimethoxyphenyl-Fmoc-aminomethyl)phenoxyacetamidoethyl resin in Pioneer TM peptide synthesizer, and carry out peptide synthesis under nitrogen in the following order:

[0074] 1. Solvate the resin in DMF for 5 minutes;

[0075] 2. Treat the resin with 20% piperidine in DMF for about 15 minutes to remove the protecting group Fmoc on the resin grafted group (or on the resin-bound amino acid α-amino group);

[0076] 3. Wash the resin with DMF for about 1 minute;

[0077] 4. Activate the α-carboxyl group of the first amino acid Arg at the C-terminal with a 0.2M solution of HBTU and HOBT in DMSO-NMP (N-methylpyrrolidone) and a 0.4M solution of diisopropylethylamine i...

Embodiment 3

[0094] Example 3. Homology Analysis of FpAT and VEGF

[0095] Using the analysis program (http: / / www.ebi.ac.uk / Tools / Sequence Analysis-ClustalW), the homology between FpAT and VEGF was analyzed according to the default parameters. The analysis results are as follows:

[0096] FpAT -----DSG--------------EG-------------DFL------------8

[0097] RRGAEESGPPHSPSRRGSASRAGPGRASETMNFLLSWVHWSLALLLYLHH 200

[0098] :** * :**

[0099] VEGF -----AEGGG-----------VR--------------------------15

[0100] AKWSQAAPMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIE 250

[0101] ***** *:

[0102] It can be seen that the six amino acids Leu-Ala-Glu-Gly-Gly-Gly and at least the five amino acids Ala-Glu-Gly-Gly-Gly are important sequences of the small peptide.

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 present invention relates to a small peptide for treatment of angiogenesis diseases and also relates to multi nucleotide for coding the small peptide, carriers and cells containing the multi nucleotide, and methods and drug combinations using the peptide, multi nucleotide, carriers or cells to treat angiogenesis diseases.

Description

technical field [0001] The present invention relates to small peptides and applications thereof, specifically, small peptides that can be used to treat angiogenic diseases, polynucleotides encoding these small peptides, vectors and cells containing the polynucleotides, and the use of these peptides, Methods and pharmaceutical compositions for treating angiogenic diseases with polynucleotides, vectors or cells. Background technique [0002] Tumor is one of the persistent diseases that endanger human health. There are many ways to treat tumors. Anti-angiogenesis therapy developed based on the relationship between angiogenesis and tumor growth and metastasis is a relatively promising method and has become a new treatment for cancer. hope. As early as the 1970s, Folkman proposed that angiogenesis is the biological basis and important link of malignant transformation, growth and metastasis of tumors, and proposed that inhibitors of angiogenesis may become a new and valuable mean...

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 Applications(China)
IPC IPC(8): C07K7/04A61K38/08A61K38/10A61P35/00C07K19/00A61K38/16C12N15/11C12N15/63C12N15/86
CPCC07K14/52A61K38/00C07K7/08A61P35/00
Inventor 寿成超苏亚辉
Owner BEIJING SAISHENG PHARMA
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