Anti-integrin alpha8beta1 Antibody for Ligand Binding Inhibition

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Solution Overview

Problem

Current techniques lack a functional inhibitor or therapeutic/diagnostic agent targeting integrin α8β1, which is involved in diseases and tissue morphogenesis, and existing antibodies are limited in their ability to inhibit integrin α8β1 function or cross-reactivity with multiple species.

Innovation Solution

Development of an anti-integrin α8β1 antibody that inhibits the binding between integrin α8β1 and its ligand, with cross-reactivity towards mammals, including humans and mice, and a process for producing such antibodies using immunization and panning selection.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Reliability

If conventional antibodies against integrin α8β1 are used, then detection by Western blotting and flow cytometry is possible, but functional inhibition of integrin α8β1 binding cannot be achieved

Engineering Contradiction:
Improvefunctional inhibition capabilityVSAvoidavailability of therapeutic/diagnostic agent
Core Design Contradiction:
ReliabilityVSEase of manufacture

Solution Approach 1:

The patent modifies the antibody's binding characteristics by selecting and characterizing antibodies with specific binding affinities and modes (competitive vs non-competitive inhibition). This parameter change enables the antibody to function as a therapeutic agent that inhibits integrin α8β1-ligand binding, transforming it from a mere detection tool to a functional inhibitor.

Inventive Principle:
Principle #35Parameter changes

Solution Approach 2:

The antibody serves as an intermediary substance that blocks the interaction between integrin α8β1 and its ligands (such as fibronectin, vitronectin, osteopontin). By introducing this intermediary, the patent achieves functional inhibition of the integrin-ligand binding pathway, enabling therapeutic effects.

Inventive Principle:
Principle #24Intermediary (Mediator)

2Adaptability or versatility

If species-specific antibodies are used, then high specificity for that species is achieved, but cross-reactivity with multiple species is limited

Engineering Contradiction:
Improvecross-species reactivityVSAvoidspecificity for particular species
Core Design Contradiction:
Adaptability or versatilityVSMeasurement precision

Solution Approach 1:

The patent develops antibodies that possess universal binding capability across multiple species (mouse, rat, human) while maintaining sufficient specificity for each. This multi-functionality allows a single antibody to serve as a therapeutic agent applicable to different species, achieving both cross-reactivity and species-specific precision when needed.

Inventive Principle:
Principle #6Universality (Multi-functionality)

3Reliability

If existing integrin-targeting antibodies are used, then some binding activity is achieved, but novel mechanism of action for therapeutic effect is not obtained

Engineering Contradiction:
Improvetherapeutic effectVSAvoidcomplexity of mechanism of action
Core Design Contradiction:
ReliabilityVSDevice complexity

Solution Approach 1:

The patent extracts and isolates the critical binding interface between the antibody and integrin α8β1, focusing on the complementarity determining regions (CDRs) that mediate ligand competition. By concentrating on this specific interaction mechanism, the patent achieves a clear and direct therapeutic effect through ligand competition without complex multi-target mechanisms.

Inventive Principle:
Principle #2Taking out (Extraction)

Data Source

PatentUS8658770B2Integrin alpha 8-beta 1-specific monoclonal antibody
Publication Date: 2014.02.25 HIROSHIMA UNIVERSITY
  • US8658770B2 patent drawing
  • US8658770B2 patent drawing
  • US8658770B2 patent drawing

AI summary

[Object] To obtain an anti-integrin α8β1 antibody which binds to integrin α8β1 derived from mammals of different species. Also, to obtain an anti-integrin α8β1 antibody which inhibits binding between integrin α8β1 and its ligand.[Solution] Anti-integrin α8β1 antibodies which bind to integrin α8β1 derived from mammals of different species have been obtained. In addition, inhibitors, which contain an anti-integrin α8β1 antibody, of binding between integrin α8β1 and its ligand have been obtained.