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

Antigenic peptides for prevention and treatment of cancer

A technology of antigenic peptides and peptides, applied in various peptide fields of immunotherapy and cancer immunotherapy, can solve the problems of limited number of human tumor antigens and autoimmune side effects.

Pending Publication Date: 2020-12-22
ENTEROME
View PDF12 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0009] However, the number of human tumor antigens on which cancer vaccines can be developed is limited
Specifically, antigens derived from mutated or modified self-proteins can induce immune tolerance and / or unwanted autoimmune side effects

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
  • Antigenic peptides for prevention and treatment of cancer
  • Antigenic peptides for prevention and treatment of cancer
  • Antigenic peptides for prevention and treatment of cancer

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0605] Example 1: Antigenic peptides have superior binding affinity compared to human peptides.

[0606] Computer simulations (in silico) predicted the binding affinities of exemplary antigenic peptides of the invention and corresponding human tumor antigen (human reference peptide) fragments to MHC class I.

[0607] This prediction has been made by using the NetMHC 4.0 server (http: / / www.cbs.dtu.dk / services / NetMHC / ) and as Andreatta M, Nielsen MGapped sequence alignment using artificialneural networks: application to the MHC class I system. Bioinformatics( 2016) Feb 15;32(4):511-7. This approach generates high accuracy predictions of major histocompatibility complex (MHC): peptide binding, specifically peptides 8-11 amino acids in length.

[0608] Table 2 below shows the results, ie information on the prediction of peptide-MHC class I binding.

[0609]

[0610]

[0611]

[0612]

[0613]

[0614]

[0615]

[0616]

[0617]

[0618]

[0619] ...

Embodiment 2

[0627] Example 2: Antigenic peptides have superior affinity to HLA-A*0201 alleles.

[0628] Then, the binding affinity of each selected antigen peptide and the corresponding human tumor antigen (human reference peptide) fragment to the HLA-A*0201 allele was confirmed in vitro. That is, the sequence SEQ ID NO:32 ("FMLGEFLKL", also referred to herein as BIRC5-B1); SEQ ID NO:30 ("YTLGEFLYI", also referred to herein as BIRC5-B2); and SEQ ID NO :31 ("GLLGEFLQI", also referred to herein as BIRC5-B3) antigenic peptide was compared with the corresponding reference human peptide derived from BIRC5 ("LTLGEFLKL", SEQ ID NO: 593, also referred to herein as BIRC5-H) Compare. In addition, the antigenic peptide of the sequence SEQ ID NO:97 ("LLLSAALSV", also referred to herein as CHI3L1 B); and SEQ ID NO:87 ("YLLSAALTI", also referred to herein as CHI3L1 B3) is identical to that derived from CHI3L1 ("LLLSAALSA", SEQ ID NO: 617, also referred to herein as CHI3L1 H) for comparison. In add...

Embodiment 3

[0648] Example 3: In the ELISPOT-IFNγ assay, vaccination of mice with antigenic peptides according to the invention induces Enhanced T cell response.

[0649] a. Materials and methods

[0650] A.1 Mouse model

[0651] The immunization protocol is shown in Figure 7 middle. Briefly, HLA-A2 humanized mice (HLA-A2(CB6F1-Tg(HLA-A*0201 / H2-K b)A*0201) were randomly assigned (based on mouse sex and age) to experimental groups, where each group was treated with the same helper peptide (h-pAg T13L; sequence: TPPAYRPPNAPIL; SEQ ID NO: 860; Bhasin M, Singh H, Raghava GP (2003) MHCBN: a comprehensive database of MHC binding and non-binding peptides. Bioinformatics 19:665–666) (summarized in Table 5 below) combined specific vaccination peptide (vacc-pAg) immunization. The vacc-pAg was compared in pairs (Group 1 vs. Group 2, Group 1 vs. Group 3; Group 1 vs. Group 4; Group 5 vs. Group 6; Group 7 vs. Group 8; Group 9 vs. Group 10). Thus, each wave compares native and optimized for...

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 antigen-based immunotherapy, in particular cancer immunotherapy. In particular, the present invention provides antigenic peptides, which are distinct from, but have amino acid similarity to, fragments of human tumor antigens. The present invention further provides immunogenic compounds, nanoparticles, cells and pharmaceutical compositions comprising such antigenicpeptides and nucleic acids encoding such antigenic peptides.

Description

technical field [0001] The present invention relates to the field of cancer therapy, more particularly by means of immunotherapy. Specifically, the present invention provides various peptides useful for cancer immunotherapy. Background technique [0002] Cancer is one of the leading causes of death worldwide. According to the World Health Organization (WHO), in 2012 alone, 14 million new cases and 8.2 million cancer-related deaths were reported worldwide, and the number of new cancer cases is expected to increase by about 70%. So far, more than 60% of the world's annual new cases occur in Africa, Asia, and Central and South America. These regions also account for 70% of the world's cancer deaths. In men, the five most common cancer sites were lung, prostate, colorectal, stomach and liver. In women it is the breasts, colorectum, lungs, cervix and stomach. [0003] Cancer has long been controlled through surgery, radiation therapy, cytotoxic chemotherapy, and endocrine m...

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): A61K39/00
CPCA61K39/0011A61K39/001119A61K39/00115A61K39/001152A61K39/001154A61K2039/55566A61P35/00C07K14/4748
Inventor L·切恩C·邦尼F·斯特鲁齐
Owner ENTEROME
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