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Methods for purifying heterodimeric, multispecific antibodies

A multi-specificity and antibody technology, applied in the field of purification of heterodimeric multi-specific antibodies, can solve unmet problems

Pending Publication Date: 2021-05-25
TENEOBIO INC
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

There are various methods known in the art for purifying antibodies, however, there remains an unmet need for alternative chromatographic processes capable of isolating and purifying multispecific antibodies from aggregates and complexes can be formed, for example, due to process-driven modifications or manufacturing conditions

Method used

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  • Methods for purifying heterodimeric, multispecific antibodies
  • Methods for purifying heterodimeric, multispecific antibodies
  • Methods for purifying heterodimeric, multispecific antibodies

Examples

Experimental program
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Effect test

Embodiment 1

[0151] Example 1: Purification of anti-CD3-BCMA bispecific antibody

[0152] figure 2 The BsAb depicted in CD3-BCMA was purified as described below. BsAb CD3-BCMA is a bispecific antibody and is structurally a trimeric in which one arm (e.g., the CD3 binding arm) contains both an intact human heavy chain and a kappa light chain, while the other arm (e.g., BCMA arm) (derived from UniRat TM technology) then consists of a human heavy chain (where one or more VH domains are directly fused to a CH domain (including, eg, hinge-CH2-CH3), and lacks a CH1 domain). The variable domain sequences comprising BsAb CD3-BCMA are shown in Table 1 below. Specifically, BsAb CD3-BCMA is a fully human IgG4 bispecific monoclonal antibody with two heavy chains (HC-1 and HC-2) and one kappa light chain (κ LC) and is acid labile. Correct pairing of heavy chains can be achieved by knobs-into-holes technology. The CD3 arm contains HC-1 and κLC and binds the T cell receptor CD3. The TAA or BCMA ar...

Embodiment 2

[0171] Example 2: Purification of bispecific antibodies comprising only heavy chain binding units

[0172]According to the methods described herein, a bispecific antibody is purified from a mixture comprising antibodies comprising a first binding unit and a second binding unit each comprising only The heavy chain variable region of a heavy chain antibody. The antibody is immobilized by contacting the mixture comprising the bispecific antibody with the first affinity chromatography material. The antibody is eluted with an elution buffer comprising an anti-aggregation composition comprising a polyol as described herein, thereby reducing aggregation of the bispecific antibody in the elution pool.

Embodiment 3

[0173] Example 3: Purification of bispecific antibodies comprising heavy chain / light chain combining units

[0174] Immobilizing the antibody by contacting a bispecific antibody comprising a first binding unit and a second binding unit each comprising a heavy chain variable region of the antibody and an antibody light chain variable region. The antibody is eluted with an elution buffer comprising an anti-aggregation composition comprising a polyol as described herein, thereby reducing aggregation of the bispecific antibody in the elution pool.

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Abstract

Methods for purifying heterodimeric, multispecific antibodies from solution are provided.

Description

[0001] Cross References to Related Applications [0002] This application claims the benefit of priority to the purposes of U.S. Provisional Patent Application No. 62 / 734,566, filed September 21, 2018, and U.S. Provisional Patent Application No. 62 / 742,821, filed October 8, 2018, the disclosures of which are incorporated by reference method is incorporated into this article as a whole. technical field [0003] The present invention relates to methods for purifying heterodimeric multispecific antibodies from solution. Background technique [0004] Bispecific antibodies (BsAbs) are an important new class of protein therapeutics. BsAbs are designed to recognize and bind two different antigens, often with the goal of retargeting immune effector cells to kill cancer cells. Currently, two BsAbs are approved as therapeutic agents by the European Medicines Agency (EMA) and one by the US Food and Drug Administration (FDA). Typically, capture using conventional protein A chromatogr...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): C07K16/28A61P35/00
CPCC07K16/2878C07K16/2809C07K2317/21C07K2317/35C07K2317/52A61P35/00B01D15/3804C07K1/22C07K2317/31C07K16/30B01D15/3809
Inventor B·约根森U·谢伦伯格
Owner TENEOBIO INC
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