Anti-TSLP Receptor Antibody CDR Modifications

Resolve Bottlenecks,
Find Innovative Solutions
Generate Solutions

Solution Overview

Problem

Current anti-human TSLP receptor antibodies have limitations in neutralizing activity, which affects their efficacy in treating allergic inflammatory diseases such as asthma and systemic sclerosis, and there is a need for an antibody with enhanced binding and neutralizing capabilities to reduce dosage and medical expenses.

Innovation Solution

Development of an anti-human TSLP receptor antibody with a heavy chain variable region consisting of amino acid sequences 1 to 118 and a light chain variable region consisting of amino acid sequences 1 to 108, along with modifications such as glutamic acid modification to pyroglutamic acid, to enhance binding and neutralizing activity.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Reliability

If conventional anti-human TSLP receptor antibodies are used, then binding activity is achieved, but neutralizing activity is insufficient

Engineering Contradiction:
Improveneutralizing activityVSAvoidantibody structure
Core Design Contradiction:
ReliabilityVSDevice complexity

Solution Approach 1:

The patent applies parameter changes by modifying the antibody's amino acid sequence parameters. Specifically, it identifies critical amino acid residues in the CDR regions and modifies them to enhance neutralizing activity while maintaining binding activity. This resolves the contradiction by changing the molecular parameters of the antibody to achieve superior therapeutic effect.

Inventive Principle:
Principle #35Parameter changes

2Reliability

If higher dosage of antibody is used to compensate for low neutralizing activity, then therapeutic effect is maintained, but medical expenses increase

Engineering Contradiction:
Improvetherapeutic effectVSAvoiddosage
Core Design Contradiction:
ReliabilityVSQuantity of substance

Solution Approach 1:

The patent modifies the antibody's amino acid composition to enhance its neutralizing potency, thereby reducing the quantity required for effective treatment. The optimized antibody structure achieves higher therapeutic effect at lower dosages, directly addressing the contradiction between therapeutic efficacy and dosage quantity.

Inventive Principle:
Principle #35Parameter changes

3Reliability

If antibody structure is optimized for higher neutralizing activity, then therapeutic efficacy improves, but development complexity increases

Engineering Contradiction:
Improveneutralizing activityVSAvoidantibody development process
Core Design Contradiction:
ReliabilityVSDevice complexity

Solution Approach 1:

The patent applies local quality by focusing modifications on specific critical amino acid residues within the CDR regions rather than redesigning the entire antibody structure. This targeted approach enhances neutralizing activity while minimizing development complexity, as only specific local regions are optimized based on structural analysis and functional data.

Inventive Principle:
Principle #3Local quality

Data Source

PatentEP3031913B1Novel Anti-human TSLP receptor antibody
Publication Date: 2019.04.17 ASTELLAS PHARMA INC
  • EP3031913B1 patent drawingFigure 1
  • EP3031913B1 patent drawingFigure 2
  • EP3031913B1 patent drawingFigure 3

AI summary

[Problem] To provide an anti-human TSLP receptor antibody that specifically binds to human TSLP receptor and inhibits an action of human TSLP through human TSLP receptor. [Means for Solution] An anti-human TSLP receptor antibody had been studied by the present inventors, and an anti-human TSLP receptor antibody comprising a heavy chain variable region consisting of the amino acid sequence of amino acid numbers 1 to 118 of SEQ ID NO: 1 and a light chain variable region consisting of the amino acid sequence of amino acid numbers 1 to 108 of SEQ ID NO: 3 was provided. It was revealed that the anti-human TSLP receptor antibody inhibits expression of TARC mRNA induced by TSLP and production of MDC proteins, and suppressed an allergic reaction in a monkey Ascaris antigen sensitization model, and then the present invention was completed.