Antibody-Bound Nanoparticles via Modular Polypeptide Self-Assembly

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Solution Overview

Problem

Current methods lack the precision to form ordered and structurally homogeneous antibody-bound nanoparticle structures.

Innovation Solution

The development of polypeptides with specific amino acid sequences that can assemble into polymers and bind to the constant region of IgG antibodies, forming precise higher-order structures such as dihedral, tetrahedral, octahedral, or icosahedral symmetries.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Manufacturing precision

If conventional methods are used to form antibody-bound nanoparticle structures, then the structures can be formed, but they lack precision and structural homogeneity

Engineering Contradiction:
Improvestructural homogeneityVSAvoidmethod complexity
Core Design Contradiction:
Manufacturing precisionVSEase of manufacture

Solution Approach 1:

The polypeptide is divided into distinct functional domains: an Fc-binding domain (comprising helical repeat proteins) and an oligomerization domain. This segmentation allows independent optimization of antibody binding and self-assembly properties, enabling precise control over nanoparticle structure while simplifying the manufacturing process through modular design

Inventive Principle:
Principle #1Segmentation

Solution Approach 2:

The invention controls the degree of identity of the oligomerization domain (50-100% identity to reference sequences) to precisely tune self-assembly behavior. By adjusting this parameter, the patent achieves controlled formation of homogeneous nanoparticle structures with specific symmetries (dihedral, tetrahedral, octahedral, or icosahedral)

Inventive Principle:
Principle #35Parameter changes

2Reliability

If antibodies are oligomerized to enhance avidity and receptor clustering, then therapeutic efficacy is improved, but precise formation of ordered structures is not achieved

Engineering Contradiction:
Improvetherapeutic efficacyVSAvoidstructural order
Core Design Contradiction:
ReliabilityVSManufacturing precision

Solution Approach 1:

The Fc-binding domain acts as an intermediary that mediates between the antibody Fc region and the oligomerization domain. This intermediary component enables controlled oligomerization by providing a specific binding interface that directs assembly into ordered structures while maintaining high avidity through multivalent antibody binding

Inventive Principle:
Principle #24Intermediary (Mediator)

Solution Approach 2:

The nanoparticle structures are composite assemblies comprising multiple components: antibodies, Fc-binding domains, and oligomerization domains. This composite architecture combines the high affinity of antibodies with the self-assembly capabilities of the oligomerization domain, achieving both therapeutic efficacy and structural order

Inventive Principle:
Principle #40Composite materials

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

This approach enables the creation of monodisperse, cage-like nanoparticle structures that can activate specific cellular signaling pathways and enhance therapeutic or diagnostic efficacy.

Implementation Method 1

assembling into a polymer, including but not limited to a homo-polymer

Methodology Applied
Scientific EffectSelf-assembly: Self-Assembly

Implementation Method 2

non-covalently bound via the first Fc domain to one polypeptide monomer chain of a first homo-polymer

Methodology Applied
Scientific EffectNon-covalent binding: Adsorption

Data Source

PatentUS20250049731A1Designed antibody-bound nanoparticles
Publication Date: 2025.02.13 UNIV OF WASHINGTON
  • US20250049731A1 patent drawing
  • US20250049731A1 patent drawing
  • US20250049731A1 patent drawing

AI summary

Polypeptides are disclosed comprising an (Fc) binding domain, a helical polypeptide monomer, and an oligomer domain, polymers thereof, and uses thereof.