Coferon Dimers for Intracellular Protein Binding

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Solution Overview

Problem

Current drug design approaches fail to effectively target intracellular protein-protein interactions or signaling, as antibodies are too large to enter cells, while small molecule drugs lack the specificity to bind to extended protein surfaces.

Innovation Solution

Development of therapeutic coferon dimers, comprising a phenylboronic acid linker element and a 1,2 diol binding partner linker element, which form specific binding interactions with intracellular protein targets, allowing for tight and specific binding.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Measurement precision

If antibody therapeutics are used to target protein-protein interactions, then binding specificity is improved, but molecular size increases preventing cellular penetration

Engineering Contradiction:
Improvebinding specificityVSAvoidmolecular size
Core Design Contradiction:
Measurement precisionVSWeight of moving object

Solution Approach 1:

The antibody is segmented into smaller fragments (Fab, scFv, diabodies) that retain binding specificity while reducing molecular size to enable cellular penetration. The patent describes generating library members that are antibody fragments rather than full-length antibodies, allowing them to bind specific epitopes while being small enough to enter cells.

Inventive Principle:
Principle #1Segmentation

Solution Approach 2:

The patent uses combinatorial library generation to add diversity in the binding region while maintaining a constrained framework structure. This dimensional approach allows optimization of binding specificity through variable CDR regions while the framework provides structural stability and appropriate size for cellular penetration.

Inventive Principle:
Principle #17Another dimension (Dimensionality change)

2Weight of moving object

If small molecule drugs are used to reduce molecular size for cellular penetration, then cell entry is improved, but binding specificity to extended protein surfaces deteriorates

Engineering Contradiction:
Improvemolecular sizeVSAvoidbinding specificity
Core Design Contradiction:
Weight of moving objectVSMeasurement precision

Solution Approach 1:

The antibody fragments are composed of framework regions providing structural stability and CDR regions providing binding specificity. This composite structure combines the advantages of large molecules (specificity) with the advantages of small molecules (cellular penetration), creating a hybrid therapeutic agent.

Inventive Principle:
Principle #40Composite materials

Solution Approach 2:

The patent applies local quality by having the CDR regions provide high binding specificity to target epitopes while the framework regions provide structural support and maintain appropriate molecular size. Different regions of the antibody fragment have specialized functions that together resolve the contradiction between size and specificity.

Inventive Principle:
Principle #3Local quality

3Reliability

If combinatorial libraries are generated to improve binding diversity, then binding affinity is improved, but library complexity and screening difficulty increase

Engineering Contradiction:
Improvebinding affinityVSAvoidlibrary complexity
Core Design Contradiction:
ReliabilityVSDevice complexity

Solution Approach 1:

The patent employs phage display technology to create a dynamic library system where binding events are amplified through biological replication. High-affinity binders are enriched through iterative selection rounds, allowing the library to dynamically evolve toward higher binding affinity while managing complexity through biological selection rather than exhaustive screening.

Inventive Principle:
Principle #15Dynamics

Solution Approach 2:

The selection process incorporates feedback mechanisms where binding results from one round inform the selection strategy for subsequent rounds. High-affinity binders are identified and used to guide further library construction and selection, creating a feedback loop that systematically improves binding affinity while managing library complexity through informed iterative optimization.

Inventive Principle:
Principle #23Feedback

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 coferon dimers achieve high affinity binding to protein targets, enabling modulation of protein-protein interactions and signaling with increased specificity and reduced toxicity, and can be orally active and penetrate tumors.

Implementation Method 1

the phenylboronic acid linker element binds to the 1,2 diol binding partner linker element to form a boronate ester

Methodology Applied
Scientific EffectBoronate ester formation: Chemical Bonding

Implementation Method 2

the first diversity element binds to the target, and (3) the second diversity element binds to the target

Methodology Applied
Scientific EffectProtein-ligand binding: Van der Waals Force

Data Source

PatentEP2279291B1Coferons and methods of making and using them
Publication Date: 2019.07.03 CORNELL UNIVERSITY
  • EP2279291B1 patent drawingFigure 1
  • EP2279291B1 patent drawingFigure 2.1A~2.1K
  • EP2279291B1 patent drawingFigure 2.2L~2.2S

AI summary

A monomer useful in prepaπng therapeutic compounds includes a diversity element which potentially binds to a target molecule with a dissociation constant of less than 300 11 M and a linker element connected to the diversity element The linker element has a molecular weight less than 500 daltons, is connected, directly or indirectly through a connector, to said diversity element, and is capable of forming a reversible covalent bond or noncovalent interaction with a binding partner of the linker element The monomers can be covalently or non-covalently linked together to form a therapeutic multimer or a precursor thereof