DNA-Peptide Hybrid Molecules for Photocleavable Multivalent Binding
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Solution Overview
Problem
Existing methods for blocking protein-protein interactions lack high affinity and specificity, are not reversible, and cannot be switched on-demand, making it difficult to target multiple binding sites effectively.
Innovation Solution
Development of DNA-peptide hybrid molecules that comprise a DNA nanostructure chemically linked to target-specific binding peptides, allowing for multivalent binding and reversible interaction blocking through photocleavable linkages.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Ease of operation
If small molecule drugs or peptides are used to block protein-protein interactions, then the approach is simple and can be administered easily, but the binding affinity and specificity to the target interface are insufficient
Solution Approach 1:
The patent combines DNA nanostructures with peptide ligands to create hybrid molecules that merge the advantages of both components: the programmability and structural control of DNA with the binding specificity of peptides, achieving high-affinity blockage of protein-protein interactions
Solution Approach 2:
The invention uses composite DNA-peptide hybrid molecules where DNA nanostructures serve as scaffolds displaying multiple peptide ligands, creating a material with enhanced binding properties that neither component could achieve alone
2Reliability
If antibodies are used to block protein-protein interactions, then high binding affinity can be achieved, but the interactions cannot be reversed or switched on-demand
Solution Approach 1:
The patent introduces dynamic control through light-responsive elements that allow the DNA-peptide hybrid molecules to switch between bound and unbound states, enabling on-demand activation and reversal of protein-protein interaction blockage
Solution Approach 2:
The invention uses photocleavable linkages that change their chemical state upon light exposure, allowing reversible detachment of peptide ligands from DNA scaffolds to control binding affinity dynamically
3Ease of manufacture
If traditional methods are used to target protein interactions, then the approach is straightforward, but multiple binding sites cannot be targeted effectively with high valency
Solution Approach 1:
The patent divides the binding function into multiple independent peptide ligands displayed on a DNA scaffold, allowing each peptide to target a different binding site on the protein while maintaining overall coordination through the DNA structure
Solution Approach 2:
The invention uses the three-dimensional structural capabilities of DNA nanostructures to position multiple peptide ligands in specific spatial arrangements that match the geometry of multiple binding sites on target proteins, adding a spatial dimension to the binding strategy
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
Enhances binding affinity and specificity to protein targets, enabling spatiotemporal control over protein-protein interactions, and allows for reversible blocking using light-responsive mechanisms.
Implementation Method 1
the chemical linkage comprises a photocleavable linkage
Data Source
AI summary
The present disclosure relates to DNA-peptide hybrid molecules. In some embodiments, the DNA-peptide hybrid molecules comprise target-specific binding peptides which selectively bind to a target molecule. Methods of using DNA-peptide hybrid molecules in the treatment of diseases or disorders are also provided.