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ECM Protein Nanofibers and Nanostructures Engineered Using Surface-initiated Assembly
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Precisely patterned nanofibres made from extendable protein multiplexes
Neville P Bethel1,2,3, Andrew J Borst1,2, Fabio Parmeggiani4,5,6
1Department of Biochemistry, University of Washington, Seattle, WA, USA.
Nature Chemistry
|September 4, 2023
Summary
Researchers created modular, rigid protein oligomers with tunable symmetry for materials design. These building blocks enable the systematic construction of extendable protein fibers with precise geometric control.
Area of Science:
- Biomaterials science
- Protein engineering
- Supramolecular chemistry
Background:
- Molecular systems with cyclic and superhelical symmetry offer advantages for materials design due to their tunable lengths.
- Alpha-helical coiled coils possess such symmetry but are limited by fixed geometry and flexibility.
Purpose of the Study:
- To develop a systematic method for creating modular and rigid repeat protein oligomers.
- To engineer extendable protein fibers with precisely controlled geometry.
Main Methods:
- Designing repeat protein oligomers with coincident C2 to C8 and superhelical symmetry axes.
- Utilizing repeat propagation to extend oligomer length.
- Introducing hydrophilic surface patches to control monomer staggering in fiber formation.
Main Results:
- Successfully generated modular and rigid repeat protein oligomers with desired symmetry.
- Demonstrated the systematic design of unbounded protein fibers by controlling monomer interactions.
- Showcased precise tuning of fiber geometry through variations in repeat units and patch placement.
Conclusions:
- A systematic approach to designing modular, rigid protein oligomers with tunable symmetry has been established.
- These protein building blocks facilitate the creation of extendable, geometrically precise protein fibers.
- This work provides a versatile platform for advanced biomaterials design.
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