Self-Assembling Protein Nanostructures for Multivalent F-Protein Display
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Solution Overview
Problem
Existing methods for designing self-assembling protein nanostructures, particularly those displaying paramyxovirus and pneumovirus F proteins, have been slow to advance, limiting the development of advanced functional materials with these proteins.
Innovation Solution
The formation of nanostructures through the non-covalent interaction of first and second assemblies of polypeptides, each with high identity to specific amino acid sequences, allowing for the multivalent display of paramyxovirus and pneumovirus F proteins on the nanostructure exterior, facilitated by recombinant expression and assembly in vitro.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Productivity
If methods for designing self-assembling protein nanostructures are advanced, then the development of advanced functional materials with paramyxovirus and pneumovirus F proteins is improved, but the current slow progress limits this development
Solution Approach 1:
The patent divides the nanostructure into multiple independent polypeptide assemblies (first assemblies with SEQ ID NOS: 1-34 and second assemblies with SEQ ID NOS: 36-51) that self-assemble through non-covalent interactions. This segmentation allows modular design and accelerated development of functional materials by combining different polypeptide building blocks.
Solution Approach 2:
The polypeptide assemblies automatically self-assemble into ordered nanostructures through inherent non-covalent interactions without requiring external assembly machinery or complex processing steps. This self-assembly capability accelerates material development by eliminating time-consuming assembly procedures.
2Reliability
If multiple copies of F proteins are displayed on nanostructure exterior, then immune response is enhanced, but the complexity of designing self-assembling protein nanostructures increases
Solution Approach 1:
The patent creates universal polypeptide assemblies (first and second assemblies with specific SEQ ID NOS) that can display multiple different F proteins from paramyxovirus and pneumovirus families. These assemblies serve multiple functions: structural organization, protein display, and immune response induction, reducing overall design complexity while maintaining effectiveness.
Solution Approach 2:
The patent combines different polypeptide assemblies (first assemblies with SEQ ID NOS: 1-34 and second assemblies with SEQ ID NOS: 36-51) into composite nanostructures that display multiple F proteins. This composite approach allows systematic design of complex immunogenic materials by combining standardized building blocks.
3Manufacturing precision
If ordered symmetric supramolecular complexes are formed through self-assembly, then matter patterning at atomic scale is achieved, but the functional and physical properties of proteins make advancement slower compared to nucleic acid-based materials
Solution Approach 1:
The patent optimizes specific parameters of the polypeptide sequences (SEQ ID NOS: 1-51) including amino acid composition, charge distribution, and hydrophobicity to enable precise self-assembly into ordered nanostructures. These parameter optimizations maintain atomic-scale patterning precision while improving assembly efficiency and development progress.
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 nanostructures effectively display multiple copies of F proteins, enhancing immune responses and providing stable, ordered structures for immunogenic applications.
Implementation Method 1
wherein the plurality of first assemblies non-covalently interact with the plurality of second assemblies to form a nanostructure
Implementation Method 2
Molecular self- and co-assembly of proteins into highly ordered, symmetric supramolecular complexes is an elegant and powerful means of patterning matter at the atomic scale
Data Source
AI summary
Disclosed herein are nanostructures and their use, where the nanostructures include(a) a plurality of first assemblies, each first assembly comprising a plurality of identical first polypeptides;(b) a plurality of second assemblies, each second assembly comprising a plurality of identical second polypeptides, wherein the second polypeptide differs from the first polypeptide;wherein the plurality of first assemblies non-covalently interact with the plurality of second assemblies to form a nanostructure; andwherein the nanostructure displays multiple copies of one or more paramyxovirus and/or pneumovirus F proteins or antigenic fragments thereof, on an exterior of the nanostructure.