Tyrosine protein kinase receptor epha2 dominant epitope complex and its preparation method and application

A technology of tyrosine protein and dominant epitope, which is applied in chemical instruments and methods, hybrid peptides, drug combinations, etc., can solve problems such as complexes that have not yet been seen, and achieve effective induction of immune responses, good development and application prospects, inhibition of The effect of tumor growth

Inactive Publication Date: 2011-11-30
FUZHOU GENERAL HOSPITAL OF NANJING MILITARY COMMAND P L A
View PDF6 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0009] But so far, there is no report on the complex composed of EphA2 epitope, transmemb

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
  • Tyrosine protein kinase receptor epha2 dominant epitope complex and its preparation method and application
  • Tyrosine protein kinase receptor epha2 dominant epitope complex and its preparation method and application
  • Tyrosine protein kinase receptor epha2 dominant epitope complex and its preparation method and application

Examples

Experimental program
Comparison scheme
Effect test

Example Embodiment

[0027] In order to make the objectives, technical solutions, and advantages of the present invention clearer, the preferred embodiments of the present invention will be described in detail below with reference to the accompanying drawings. The experimental methods that do not specify specific conditions in the preferred embodiments usually follow conventional conditions, such as those described in the Molecular Cloning Experiment Guide (third edition, J. Sambrook et al., translated by Huang Peitang et al., Science Press, 2002) Or in accordance with the conditions recommended by the manufacturer.

[0028] 1. Preparation of EphA2 dominant epitope complex

[0029] 1. Prediction of EphA2 dominant epitope

[0030] A super motif refers to a peptide motif composed of the same and similar anchor residues in the antigen peptides accepted by HLA allogeneic molecules of the same HLA family or even different families. The main anchor residues of the super motif are the amino acid residues at ...

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 a mesylate protein kinase receptor EphA2 dominant epitope compound and a preparation method and application thereof in preparing a therapeutic vaccine for tumor. The compound is prepared from EphA258-66 epitope fusion peptide, EphA2550-558 epitope fusion peptide and EphA2253-261 epitope fusion peptide in mol ratio of 1:1:1 and an LIGHT gene recombinant eukaryotic expression vector; the EphA258-66/550-558/253-261 epitope fusion peptides are respectively prepared from EphA258-66/550-558/253-261 epitopes and a transmembrane sequence HIV-Tat49-57, an endoplasmic reticulum retention signal sequence KDEL and a linker sequence AAY; the combination of the three EphA2 dominant epitopes can effectively overcome the deficiency of a single epitope on immune effect; the three epitope fusion peptides can enter the kytoplasm under the guide action of the transmembrane sequence, target the endoplasmic reticulum under the action of the endoplasmic reticulum retention signal sequence, and efficiently enter an MHC-I (major histocompatibility complex-class I) antigen presenting route; and the LIGHT gene recombinant eukaryotic expression vector can express LIGHT protein in vivoand play a role of a molecular adjuvant to promote the immune response of epitope specific T cells.

Description

technical field [0001] The invention belongs to the field of biomedicine and relates to an antigen epitope complex, in particular to a dominant epitope complex of tyrosine protein kinase receptor EphA2, and also relates to a preparation method and application of the dominant epitope complex. Background technique [0002] A lot of progress has been made in the treatment of malignant tumors, but the minimal residual lesions are still difficult to be completely removed by current radiotherapy, chemotherapy, surgery and other programs. Applying tumor immunotherapy to stimulate the body's immune surveillance system to eliminate residual tumor cells may completely cure the tumor. Therefore, the development of tumor vaccines has become one of the current research hotspots. [0003] In view of the decreased immunogenicity of tumor antigens in the body, resulting in insufficient activation of specific cellular immunity and peripheral immune tolerance, the general idea of ​​tumor vac...

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): A61K39/00A61K39/39C07K19/00A61P35/00
Inventor 陈宏颉王守森郑兆聪袁邦青王如密高进喜赵琳
Owner FUZHOU GENERAL HOSPITAL OF NANJING MILITARY COMMAND P L A
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

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

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap