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

Oligopeptide with breast cancer resisting activity and application thereof

An anti-breast cancer, breast cancer cell technology, applied to oligopeptide with anti-breast cancer activity and its application, oligopeptide and its application field, can solve the problems of high cost and long cycle, achieve small molecular weight and easy industrialization , the effect of inhibiting tumor proliferation

Inactive Publication Date: 2014-07-16
QINGDAO HISER MEDICAL CENT
View PDF2 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Benefits of technology

This patented new compound was found by researchers at University College London (UK) during their study testing its ability to prevent or treat brain neoplasms like lung carcinoma without causing damage to healthy tissues. It could also have potential use in developing other types of medications such as chemotherapy agents targeting certain specific proteins involved in regulating gene expression.

Problems solved by technology

Biomolecule synthetic techniques provide technical solutions for producing peptoids, specifically oligopexanes, as well as complex structures containing diverse types of atoms like metals and nonlinear ones. However, current methods require expensive materials and complicated procedures, leading to low yields due to impurities generated during production. Additionally, existing methods suffer from poor selectivity and sensitivity issues when trying to combine them effectively together without compromising their functions themselves.

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
  • Oligopeptide with breast cancer resisting activity and application thereof
  • Oligopeptide with breast cancer resisting activity and application thereof
  • Oligopeptide with breast cancer resisting activity and application thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0024] Design and synthesis of oligopeptides

[0025] 1. Extract the major international antimicrobial peptide database (http: / / aps.unmc.edu / AP / main.php; http: / / penbase.immunaqua.com / ; http: / / www.bbcm.univ.trieste.it / ; Http: / / www.imtech.res.in / raghava / antibp / ), analyze the corresponding relationship between its primary structure and activity, and design the artificial short peptide sequence.

[0026] 2. Use the protein analysis database http: / / www.expasy.org / to analyze the similarity of the secondary structure between the oligopeptide sequence with known activity and the designed oligopeptide sequence, and to modify the design sequence in combination with other physical and chemical parameter predictions .

[0027] 3. Send the oligopeptide sequence to the biological company for synthesis or use an automatic oligopeptide synthesizer to synthesize the full sequence. The purity of HPLC detection is greater than 96%, and the quality of oligopeptide synthesis is determined by mass spe...

Embodiment 2

[0031] Identification of oligopeptides

[0032] P1222 oligopeptide was hydrolyzed by 5.7mol / L HCl for 16 hours, and analyzed for amino acid. It was found that it contained 9 kinds of amino acids including Phe, Thr, Gln, Tyr, Pro, Lys, Arg, Gly, Ser, etc. The molar ratio was Phe: Thr : Gln: Tyr: Pro: Lys: Arg: Gly: Ser = 1:1:1:1:1:1:1:1:1. After amino acid sequence analysis, the sequence is Phe-Thr-Gln-Tyr-Pro-Lys-Arg-Gly-Ser. A peak was determined by electrospray mass spectrometry, and its molecular weight was 1083.21.

Embodiment 3

[0034] Detection of tumor suppressor activity of P1222 oligopeptide in vitro by MTT method

[0035] 2.1 Materials and reagents

[0036] 1) P1222 oligopeptide, synthesized by Shanghai Shenggong Biological Engineering Technology Service Co., Ltd.

[0037] 2) Human breast cancer cell lines MCF-7 and MDA-MB-231, human normal breast cells MCF-10A, were purchased from the Cell Resource Center of Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences.

[0038] 3) RPMI1640 medium, DMEM medium, and newborn calf serum are all products of GIBCO, USA.

[0039] 4) Dimethyl sulfoxide (DMSO), tetramethyl azoazole (MTT) and trypsin are products of Sigma.

[0040] 2.2 Experiment

[0041] 1) Dilute P1222 oligopeptide to an initial concentration of 1 mM with a diluent (sterile PBS, or sterile water, or corresponding cell culture medium), filter and sterilize, and freeze at -20°C after aliquoting.

[0042] 2) Cell culture: The cancer cells are cultured in RPMI1640 culture medium (containing ...

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 an oligopeptide with breast cancer resisting activity. A sequence of the oligopeptide is Phe-Thr-Gln-Tyr-Pro-Lys-Arg-Gly-Ser. The oligopeptide is capable of selectively inhibiting the growth of in vitro breast cancer cells at a lower concentration without influencing the growth of normal breast cells. In vivo experiments indicate that the oligopeptide has a strong function of inhibiting the growth and the proliferation of cancer cells, and shows a remarkable dose-effect relationship. Due to a safe, efficient and perfect cancer resisting effect, the oligopeptide can be used for preparing an anti-cancer medicine, and has a better application prospect.

Description

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

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
Owner QINGDAO HISER MEDICAL CENT
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