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

HUMANIZED ANTI-SIRPalpha ANTIBODIES

A humanized and antibody technology, applied in the direction of antibodies, antibody medical components, anti-tumor drugs, etc., can solve the problem of not promoting the anti-tumor activity of immune effector cells

Pending Publication Date: 2021-09-17
БАЙОНДИС Б. В.
View PDF15 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Likewise, the specificity of the humanized antibody HEFLB disclosed in WO2017 / 178653 is too strong because the antibody does not bind to SIRPα 1 Binds (measured by SPR; see Examples section) and does not promote 1 Antitumor activity of immune effector cells in carriers, even in the presence of SIRPα BIT When an allele of ( image 3 )

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
  • HUMANIZED ANTI-SIRPalpha ANTIBODIES
  • HUMANIZED ANTI-SIRPalpha ANTIBODIES
  • HUMANIZED ANTI-SIRPalpha ANTIBODIES

Examples

Experimental program
Comparison scheme
Effect test

Embodiment

[0169] 1. Transient Expression of Antibodies

[0170] a) Preparation of cDNA constructs and expression vectors

[0171] The heavy chain variable region (HCVR) amino acid sequences of the antibodies were each linked at the N-terminus to a leader sequence (SEQ ID NO: 28 for antibodies 1 to 13) and at the C-terminus to a human IgG according to SEQ ID NO: 25 1 HC LALA constant domain linkage (computer simulation). The HCVR amino acid sequences of antibodies 12C4, 12C4-LALA, 29AM4-5-LALA or KWAR23-LALA were each linked at the N-terminus to the HAVT20 leader sequence (SEQ ID NO:27) and at the C-terminus to the HAVT20 leader sequence (SEQ ID NO:25) human IgG 1 HC LALA or wild type human IgG 1 The constant domains of HC (SEQ ID NO: 24) are linked. KWAR23 has the standard adalimumab heavy chain constant domain but lacks the LALA mutation. The HEFLB heavy chain was IgG4 and was used as disclosed in SEQ ID NO: 42 of WO 2017 / 178653. The resulting amino acid sequence was back-trans...

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 humanized antibodies against SIRPalpha that are suitable for use in anti-cancer therapy. The invention further relates to the use of the humanized anti-SIRPalpha antibodies in the treatment of human solid tumours and haematological malignancies, optionally in combination with further anti-cancer therapeutics.

Description

technical field [0001] The present invention relates to humanized antibodies against SIRPα and the use of these antibodies (optionally in combination with anti-cancer therapeutics) in the treatment of cancer. Background technique [0002] Therapeutic antibodies that recognize antigens on tumor cells have been available to treat cancer since the late 1990s. These therapeutic antibodies can act on malignant cells through different pathways. Signaling pathways triggered by the binding of antibodies to their targets on malignant cells result in inhibition of cell proliferation or apoptosis. The Fc region of therapeutic antibodies can trigger complement dependent cytotoxicity (CDC), antibody-dependent cellular cytotoxicity (ADCC) and / or antibody-dependent cellular phagocytosis , ADCP). Another possible mechanism could be the antibody-dependent induction of T cells (CD8 + and / or CD4 + ) anti-tumor response (antibody-dependent antigen presentation (ADAP); DiLillo and Ravetch C...

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): C07K16/28A61K39/00A61P35/00
CPCC07K16/2803C07K2317/33C07K2317/72C07K2317/732C07K2317/76C07K2317/92A61K2039/505A61P35/00C07K16/2896C07K2317/24C07K2317/565A61K45/06C12N5/10A61K39/395
Inventor 海斯贝特斯·弗朗西斯库斯·玛丽亚·费尔海登
Owner БАЙОНДИС Б. В.
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