CBM32-Derived Affinity Scaffold for Antibody Replacement

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Solution Overview

Problem

The complexity of antibodies makes them difficult to produce for various applications, necessitating the development of antibody-like protein substitutes with similar properties.

Innovation Solution

A CBM32-derived affinity scaffold with constant regions and variable loop regions is developed, providing a stable framework for specific binding to target molecules, allowing for the creation of proteins that can bind challenging targets with high affinity and stability.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Reliability

If traditional antibodies are used for specific binding applications, then high binding specificity is achieved, but production complexity and difficulty increase

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

Solution Approach 1:

The patent creates simplified protein substitutes that copy the essential binding function of antibodies without replicating their complex structure. The CBM32-derived affinity scaffold mimics antibody binding capabilities using a much simpler protein framework, eliminating the need for complex antibody production while maintaining specific binding to target molecules

Inventive Principle:
Principle #26Copying

Solution Approach 2:

The invention extracts only the essential binding function from antibodies, separating it from the complex immunoglobulin structure. By using CBM32 carbohydrate-binding modules, the patent isolates the core affinity-binding capability and removes the unnecessary complexity of full antibody structures, enabling simpler production while preserving binding specificity

Inventive Principle:
Principle #2Taking out (Extraction)

2Reliability

If antibody structure is maintained for binding function, then cognate cell type coordination is preserved, but structural complexity increases

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

Solution Approach 1:

The patent extracts the essential carbohydrate-binding function from the complex antibody structure, using only the necessary CBM32 modules to achieve binding. This extraction eliminates unnecessary structural elements while preserving the core binding capability needed for specific target recognition

Inventive Principle:
Principle #2Taking out (Extraction)

Solution Approach 2:

The simplified CBM32-based affinity proteins serve as functional substitutes for expensive and complex antibodies. These simpler proteins can be produced more easily and used for specific binding applications without requiring the elaborate antibody structure, making them practical alternatives for research and diagnostic purposes

Inventive Principle:
Principle #27Cheap short-living objects (Disposable)

Data Source

PatentUS10919981B2Affinity proteins and uses thereof
Publication Date: 2021.02.16 NECTAGEN
  • US10919981B2 patent drawing
  • US10919981B2 patent drawing
  • US10919981B2 patent drawing

AI summary

In general, the invention features a novel CBM32-derived affinity scaffold. In certain embodiments, the scaffold comprises two types of regions: constant regions (CRs) and variable loop regions (VLRs) as depicted in the structure in FIG. 1. We have discovered that the CRs provide structural features that enable overall conformational stability while the intervening sequences corresponding to VLRs tolerate amino acid sequence randomization.