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Anti-egfr antibodies and their uses

A technology of antibody and humanized antibody, which is applied in anti-tumor drugs, anti-receptor/cell surface antigen/cell surface determinant immunoglobulin, anti-animal/human immunoglobulin, etc., which can solve the problem of low antibody efficiency, Eliminate the low efficiency of killing cells, antigen variation and other issues, to achieve the effect of improving therapeutic efficacy

Inactive Publication Date: 2012-10-24
ABBVIE BIOTHERAPEUTICS
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Finally, with the use of e.g. Erbitux Other issues associated with tumor-specific or tumor-selective mAbs as therapeutics include antigenic variation of the tumor, inefficient cell killing after binding the mAb, inefficient penetration of the antibody into tumors, and soluble target antigen Antibody clearance (mopping up)

Method used

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  • Anti-egfr antibodies and their uses
  • Anti-egfr antibodies and their uses
  • Anti-egfr antibodies and their uses

Examples

Experimental program
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Effect test

example 1

[0254] Example 1: Comparing the Binding Affinity of Cetuximab (ERBITUX) and HU225 to EGFR

[0255] The relative binding affinities of cetuximab and hu225 to EGFR were determined by competition assay using fluorescence activated cell sorting (FACS). A431 cells were grown to 2 × 10 on a V-bottom 96-well plate 5 cells / well. Cells were washed with FACS staining buffer (FSB). Starting with an initial concentration of 10 μg / mL of each competing antibody (unlabeled cetuximab and hu225), serial 1:3 dilutions were performed. Biotin-labeled cetuximab was diluted to a final concentration of 0.5 μg / mL (obtained from titration results). Next, biotin-labeled cetuximab was mixed with various concentrations of either competing antibody, and the mixture was transferred to a 96-well plate containing A431 cells. Plates were then incubated on ice for 1 hour, followed by two washes with FSB. 25 μL of streptavidin-RPE conjugate (Biosource) diluted to 2.5 μg / mL in FSB was added to each well and...

example 2

[0257] Example 2: Identification of HU225 variants with increased affinity for EGFR

[0258] Comprehensive mutation analysis was performed on the hu225 antibody to identify mutants with increased affinity for EGFR compared to wild-type hu225. Candidate high affinity mutants with increased affinity for EGFR compared to hu225 were analyzed by FACS to demonstrate relative increased binding to EGFR compared to hu225.

[0259] 1. Materials and Methods

[0260] To determine the binding of individual variants to EGFR, under subsaturated conditions (below K D ), and the degree of binding was quantified by FACS. Individual hu225 variants were constructed in mammalian cell surface display vectors (Akamatsu et al., 2007, J. Immunol. Methods 327(1-2):40-52) and transfected into in human cell lines. 50 μL of hybridoma-serum-free medium (SFM) containing 400 ng of plasmid DNA was mixed with 50 μL of hybridoma-SFM containing 1 μL of lipofectamine 2000 (Lipofectamine 2000), and incubated a...

example 3

[0265] Example 3: Further Characterization of HU225 Variants with Increased Affinity to EGFR (ELISA, ALPHALISA and BIACORE research)

[0266] 1. Materials and Methods

[0267] To determine the binding of individual variants to EGFR, under subsaturated conditions (below K D ), and the degree of binding was quantified by FACS (as described in Example 2 above), ELISA, alphaLISA and / or BIAcore.

[0268] ELISA involves the attachment of capture antibodies to a solid support, upon which an antigen-containing sample is added to a matrix or buffer suitable to minimize attachment to the solid phase. Enzyme-labeled antibodies are then added to detect and determine binding affinity. ELISA can be used to determine the binding affinity of individual variants (eg, anti-EGFR antibodies or antibody-binding fragments of the invention) to EGFR. See, eg, Patel et al., Anticancer Research 27, No. 5A:3355-3366, 2007; and Nix et al., "Immunoassays, a Practical Approach )”, J.P. Gosling, ed., pp...

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Abstract

The present invention relates to antibodies directed to EGFR and uses of such antibodies, for example, to treat diseases associated with the activity and / or overproduction of EGFR.

Description

[0001] Cross References to Related Applications [0002] This application claims the benefit of US Provisional Application No. 61 / 255,632, filed October 28, 2009, the contents of which are hereby incorporated by reference in their entirety. [0003] sequence listing [0004] This application contains a Sequence Listing, which has been filed in ASCII format and is hereby incorporated by reference in its entirety. Said ASCII copy, created on October 26, 2010, is named 38149322.txt and is 113,333 bytes in size. technical field [0005] The present invention relates to anti-EGFR antibodies, pharmaceutical compositions comprising anti-EGFR antibodies and therapeutic uses of said antibodies. Background technique [0006] Monoclonal antibody therapy presents an opportunity to target and destroy tumors using antibodies engineered to target tumor-specific antigens. In general, monoclonal antibody therapy stimulates a patient's immune system to attack malignant tumor cells or pr...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): C07K16/28
CPCC07K16/2863C07K2317/565C07K2317/92C07K2317/24A61P35/00
Inventor 赤松谦子罗伯特·B·迪布里吉大卫·B·鲍尔斯
Owner ABBVIE BIOTHERAPEUTICS
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