Anti-LRRC15 ADC Antibody for Epitope-Specific Tumor Targeting

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Solution Overview

Problem

There is a need for antibodies that effectively target LRRC15 for cancer treatment, as existing anti-LRRC15 antibody-drug conjugates have not been adequately developed, and there is a lack of approved anticancer agents targeting this protein.

Innovation Solution

Development of a novel anti-LRRC15 antibody that specifically binds to specific epitopes in the LRRC15 protein, particularly in regions spanning amino acid residues 22 to 315, and its conjugation with a pyrrolobenzodiazepine (PBD) derivative to form an antibody-drug conjugate, exhibiting strong antitumor activity.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Reliability

If existing anti-LRRC15 antibody-drug conjugates are used, then cancer treatment is provided, but the therapeutic efficacy is insufficient and no approved anticancer agents targeting LRRC15 are available

Engineering Contradiction:
Improvetherapeutic efficacyVSAvoidavailability of approved agents
Core Design Contradiction:
ReliabilityVSAdaptability or versatility

Solution Approach 1:

The invention segments the antibody development process by identifying and targeting specific epitope regions within LRRC15 (amino acid residues 22-315), creating specialized antibodies that bind to distinct regions. This segmentation allows for optimized therapeutic efficacy by selecting the most effective epitope-specific antibody for drug conjugation.

Inventive Principle:
Principle #1Segmentation

Solution Approach 2:

The invention changes key parameters of the antibody-drug conjugate by using pyrrolobenzodiazepine (PBD) derivative conjugation instead of conventional cytotoxic agents like MMAE. This parameter change in the drug component provides enhanced antitumor activity and distinguishes the new conjugate from existing approved agents.

Inventive Principle:
Principle #35Parameter changes

2Measurement precision

If a novel anti-LRRC15 antibody is developed to specifically bind to specific epitopes, then binding specificity is improved, but development complexity and time increase

Engineering Contradiction:
Improvebinding specificityVSAvoidantibody development complexity
Core Design Contradiction:
Measurement precisionVSDevice complexity

Solution Approach 1:

The invention applies local quality by directing antibody binding to specific local regions (epitopes) within the LRRC15 protein structure. By focusing on particular amino acid residue regions (22-315), the antibody achieves high binding specificity to critical functional domains while simplifying the overall development approach through targeted region selection.

Inventive Principle:
Principle #3Local quality

3Reliability

If an antibody-drug conjugate with strong antitumor activity is created, then therapeutic potential is enhanced, but manufacturing and conjugation complexity increases

Engineering Contradiction:
Improveantitumor activityVSAvoidconjugation process complexity
Core Design Contradiction:
ReliabilityVSEase of manufacture

Solution Approach 1:

The invention creates a composite material system by conjugating the anti-LRRC15 antibody with pyrrolobenzodiazepine (PBD) derivative drugs. This composite structure combines the target-specific binding capability of the antibody with the potent antitumor activity of PBD, achieving enhanced therapeutic effect while the modular composite design facilitates standardized manufacturing processes.

Inventive Principle:
Principle #40Composite materials

Data Source

PatentEP4703474A1Anti-LRRC15 antibody
Publication Date: 2026.03.04 DAIICHI SANKYO CO LTD
  • EP4703474A1 patent drawingFigure 1-1~1-2
  • EP4703474A1 patent drawingFigure 2-1
  • EP4703474A1 patent drawingFigure 2-2

AI summary

An object of the present invention is to provide a novel LRRC15 antibody or an antigen-binding fragment thereof that can be advantageously used in various therapeutic modalities, especially in antibody-drug conjugates (ADC), for example. The present invention provides an antibody that specifically binds to a novel epitope in LRRC15, for example.