Ubx Protein Self-Assembly for Biomaterial Morphology Control
Find Innovative SolutionsGenerate Solutions
Solution Overview
Problem
Existing technologies face challenges in producing biomaterials with improved properties such as strength, durability, and ability to form higher-order structure shapes, particularly due to limitations in sequence engineering, harsh processing conditions, and difficulties in initiating protein-based self-assembly at reduced concentrations and faster timescales.
Innovation Solution
The development of biomaterials comprising self-assembled Ultrabithorax (Ubx) protein molecules, which can form strong, durable structures capable of higher-order shape formation, using methods that require simpler conditions, lower protein concentration, and less time compared to traditional engineered biomaterials.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Ease of manufacture
If high temperatures or organic chemicals are used to stimulate protein assembly, then protein self-assembly is achieved, but active heterologous proteins cannot be incorporated and functionalization is limited
Solution Approach 1:
The patent changes the physical-chemical parameters of the assembly process by using physiological temperatures and aqueous buffers instead of high temperatures and organic solvents. This parameter change allows incorporation of active heterologous proteins while maintaining assembly capability, resolving the contradiction between ease of manufacture and adaptability.
2Reliability
If high sample concentration and extended times are used for assembly, then protein-based self-assembly is initiated, but production efficiency is reduced
Solution Approach 1:
The patent introduces polyethylene glycol (PEG) as an intermediary substance that mediates protein-protein interactions to promote self-assembly. PEG acts as a crowding agent that enhances assembly at lower protein concentrations and shorter times, resolving the contradiction between reliable assembly initiation and productivity.
3Ease of manufacture
If traditional protein-based self-assembly methods are used, then materials can be produced, but multiple higher-order structure shapes cannot be formed and encasement of non-conjugated objects is limited
Solution Approach 1:
The patent designs the protein construct with multiple functional domains that provide multi-functionality: the coiled-coil domain enables self-assembly, while additional domains allow formation of various higher-order structures and encasement of different objects. This universal design resolves the contradiction between ease of manufacture and structural versatility.
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 Ubx-based biomaterials demonstrate enhanced mechanical properties, such as elasticity and extensibility, and can be produced more efficiently, enabling various biomedical and non-biomedical applications with improved performance and reduced processing requirements.
Implementation Method 1
self-assembled Ultrabithorax (Ubx) protein molecules
Data Source
AI summary
The present disclosure relates, in some embodiments, to a composition comprising a biomaterial. A biomaterial may comprise, for example, one or more molecules capable of self-association and/or self-assembly. In some embodiments, a biomaterial may comprise one or more polypeptides and/or proteins. A biomaterial may comprise, for example, two or more self-assembled Ultrabithorax (Ubx) protein molecules. A Ubx protein, in some embodiments, may be any wild type Drosophila melanogaster Ultrabithorax protein, including any natural or non-natural isoforms (e.g., alternative splicing isoforms). The present disclosure relates, in some embodiments, to a method of making a biomaterial comprising contacting two or more Ubx protein molecules under conditions that permit self-assembly to form a first fibril and contacting the first fibril to a second fibril.