Linked Pathogen-Binding Proteins for Oral Immunotherapy 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
A protein comprising a first and second peptide with specific binding capabilities, linked by a stable linker, which maintains stability in the gastrointestinal tract and respiratory system, allowing effective binding to pathogen surface components and molecules, thereby preventing or treating infections.
Engineering Contradictions & Design Principles
Engineering 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
Solution Approach 1:
The patent combines two single-domain antibodies into a single protein molecule through a linker, creating a bivalent construct. This merging approach allows the protein to maintain binding specificity for pathogen surface components while the combined structure provides enhanced proteolytic stability in the gastrointestinal tract, resolving the contradiction between reliability of binding and stability against degradation.
Solution Approach 2:
The invention creates a composite protein structure by fusing two distinct single-domain antibody domains (each with specific binding capabilities) through a stable linker. This composite construct integrates the binding functions of individual antibodies while the combined architecture confers improved stability, allowing the protein to withstand proteolytic conditions in the stomach while maintaining pathogen targeting capability.
2Productivity
If single-domain antibodies are orally applied, then immunotherapy for gastrointestinal infections is achieved, but high doses are required due to degradation
Solution Approach 1:
By merging two single-domain antibodies into one stable bivalent protein, the invention reduces the quantity of active binding units needed. The combined structure provides both the binding specificity and the stability to survive gastric proteolysis, thereby reducing the dose requirement while maintaining immunotherapy effectiveness for gastrointestinal infections.
3Stability of the object's composition
If a stable linker is used to connect peptides, then protein stability in gastrointestinal tract is improved, but binding affinity may be affected
Solution Approach 1:
The patent applies local quality by designing a linker region with specific properties that differ from the antibody domains. The linker is engineered to provide stability and flexibility in the appropriate manner, allowing the antibody domains to maintain their binding affinity for pathogen surface components while the linker itself provides the necessary structural stability to withstand proteolytic conditions in the gastrointestinal tract.
Data Source
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.