IL10RB Single-Domain Antibodies for Close-Epitope Binding

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Solution Overview

Problem

Monoclonal antibodies, due to their large size, face challenges in effectively targeting IL10Rb receptors, particularly in assays where multiple reagents compete for close epitopes, and their use is limited in regions where maintaining a cold chain is difficult.

Innovation Solution

Development of single domain antibodies (sdAbs) that specifically bind to the extracellular domain of IL10Rb, utilizing CDRs with high sequence identity or conservative amino acid changes, enabling efficient binding and stability even in challenging environments.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Reliability

If monoclonal antibodies are used to target IL10Rb receptors, then binding specificity is achieved, but the large size limits effectiveness in assays with close epitopes and cold chain maintenance becomes difficult

Engineering Contradiction:

Improvebinding specificityVSAvoidantibody size

Core Design Contradiction:

ReliabilityVSWeight of moving object

Solution Approach 1:

The patent divides the conventional monoclonal antibody into a smaller single domain antibody fragment that retains the essential binding functionality. This segmentation allows the antibody to access close epitopes on IL10Rb receptors while maintaining binding specificity, and the reduced size eliminates cold chain requirements

Inventive Principle:

Principle #1Segmentation

Solution Approach 2:

The patent extracts only the critical binding domain from the full monoclonal antibody structure. By taking out the essential antigen-binding fragment and removing the bulky constant regions and other domains, the resulting sdAb maintains affinity for IL10Rb while achieving the small size needed for assay compatibility and thermal stability

Inventive Principle:

Principle #2Taking out (Extraction)

2Stability of the object's composition

If single domain antibodies are designed with high sequence identity CDRs, then binding stability is improved, but production complexity increases

Engineering Contradiction:

Improvebinding stabilityVSAvoidproduction complexity

Core Design Contradiction:

Stability of the object's compositionVSDevice complexity

Solution Approach 1:

The patent optimizes the sequence parameters of the CDR regions to achieve high binding stability. By carefully selecting and refining the amino acid sequences in the CDRs through rational design and screening, the patent achieves stable binding to IL10Rb while maintaining relatively simple production protocols for the sdAb constructs

Inventive Principle:

Principle #35Parameter changes

Applied Scientific Principles

This section explains which scientific principles are used to turn an abstract innovation direction into a practical engineering solution.

Function Achieved in This Case

The sdAbs provide effective targeting of IL10Rb receptors, facilitating assays and therapeutic applications with enhanced stability and ease of production, suitable for geographic areas with limited cold chain maintenance.

Implementation Method 1

single domain antibodies (sdAbs) that specifically bind to the extracellular domain of IL10Rb

Methodology Applied

Scientific EffectAntigen-antibody binding:

Data Source

PatentUS20250333521A1Il10RB binding molecules and encoding nucleic acids

Publication Date: 2025.10.30 SYNTHEKINE INC

AI summary

The present disclosure relates to biologically active molecules comprising a single domain antibody (sdAb) that specifically binds to the extracellular domain of human IL10Rb, compositions comprising such antibodies, and methods of use thereof.