Linked Pathogen-Binding Proteins for Gastrointestinal Proteolytic Stability

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Solution Overview

Problem

Existing single-domain antibodies are proteolytically degraded in the stomach, limiting their effectiveness in oral immunotherapy for gastrointestinal infections, and there is a need for stable proteins that can effectively bind to pathogen surface components and molecules to prevent or treat infections.

Innovation Solution

Development of a protein comprising two peptides with specific binding capabilities linked by a stable linker, such as a GS linker, which maintains stability in the gastrointestinal tract and allows effective binding to pathogen surface components and molecules, including toxins, thereby preventing and treating infections.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Reliability

If single-domain antibodies are used for oral immunotherapy, then binding specificity to pathogen surface components is achieved, but proteolytic degradation in the stomach reduces effectiveness

Engineering Contradiction:

Improvebinding specificityVSAvoidproteolytic stability

Core Design Contradiction:

ReliabilityVSStability of the object's composition

Solution Approach 1:

The patent merges two single-domain antibodies into a single protein construct linked by a stable linker. This combination allows the protein to bind to both F4 and F18 fimbriae simultaneously, while the linked structure provides mutual stabilization that protects against proteolytic degradation in the stomach, thereby resolving the contradiction between maintaining binding specificity and achieving proteolytic stability.

Inventive Principle:

Principle #5Merging (Combining)

Solution Approach 2:

The invention creates a composite protein structure combining two functional peptides (F4-binding and F18-binding single-domain antibodies) with a stable linker. This composite construct achieves both binding specificity for multiple pathogen components and enhanced proteolytic stability, overcoming the limitation of individual single-domain antibodies being degraded in the gastrointestinal tract.

Inventive Principle:

Principle #40Composite materials

2Reliability

If high doses of single-domain antibody are administered orally, then binding to pathogen surface components is achieved, but proteolytic degradation limits effectiveness

Engineering Contradiction:

Improvebinding capabilityVSAvoidproteolytic degradation

Core Design Contradiction:

ReliabilityVSLoss of substance

Solution Approach 1:

By merging two single-domain antibodies into a linked protein construct, the invention reduces the total amount of protein needed for effective binding. The stable linker maintains the structural integrity of both binding domains, allowing them to function together at lower doses without being completely degraded by stomach proteases, thus reducing loss of substance while maintaining binding capability.

Inventive Principle:

Principle #5Merging (Combining)

3Adaptability or versatility

If a protein construct with multiple binding peptides is created, then versatility in binding different pathogen components is improved, but structural complexity increases

Engineering Contradiction:

Improvebinding specificityVSAvoidprotein structure

Core Design Contradiction:

Adaptability or versatilityVSDevice complexity

Solution Approach 1:

The patent segments the protein construct into distinct functional modules: a first peptide for F4 binding, a second peptide for F18 binding, and a stable linker connecting them. This segmentation allows each module to be optimized for its specific binding function while the overall structure remains manageable. The modular design achieves versatility in binding different pathogen components without excessive structural complexity.

Inventive Principle:

Principle #1Segmentation

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 linked peptide protein construct maintains stability and binding affinity in harsh gastrointestinal conditions, effectively preventing biofilm formation, crosslinking pathogens, and neutralizing pathogen molecules, thus providing therapeutic benefits.

Implementation Method 1

the protein is stable in the gastrointestinal tract

Methodology Applied

Scientific EffectProteolytic stability:

Implementation Method 2

said first and said second peptides bind at least one pathogen surface component and/or at least one molecule produced by a pathogen

Methodology Applied

Scientific EffectSpecific binding:

Implementation Method 3

crosslinking pathogens

Methodology Applied

Scientific EffectCrosslinking:

Implementation Method 4

neutralizing pathogen molecules

Methodology Applied

Scientific EffectNeutralization:

Data Source

PatentUS12441783B2Pathogen binding proteins

Publication Date: 2025.10.14 BACTOLIFE AS

AI summary

The present invention relates to proteins, compositions and their use, wherein said protein comprises a first peptide having a first binding specificity, a second peptide having a second binding specificity and a linker, wherein said first and said second peptides bind at least one pathogen surface component and/or at least one molecule produced by a pathogen.