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Adaptive Recombinant Nanoworms from Genetically Encodable Star Amphiphiles
Md Shahadat Hossain1, Jingjing Ji2, Christopher J Lynch1
1Department of Chemistry, Syracuse University, 1-014 Center for Science and Technology, 111 College Place, Syracuse, New York 13244, United States.
Biomacromolecules
|December 23, 2021
Summary
Researchers engineered adaptive protein nanoworms by modifying their structure with lipids. This breakthrough allows for programmable self-assembly and temperature-responsive shape changes, expanding their use in materials and biomedicine.
Area of Science:
- Biomaterials Science
- Protein Engineering
- Nanotechnology
Background:
- Recombinant protein nanoworms show potential in nanomaterial synthesis, peptide display, and targeted drug delivery.
- Current limitations include unclear molecular design principles and narrow thermodynamic stability for nanoworm assembly.
Purpose of the Study:
- To establish design principles for programmable protein assembly into well-defined nanoworms.
- To expand the stability of protein nanoworms using topological engineering inspired by synthetic macromolecules.
Main Methods:
- Utilized post-translational modifications (PTMs) to create topologically and compositionally asymmetric lipidated proteins.
- Employed an integrated experimental and computational approach to analyze material properties.
- Investigated the impact of amphiphilic architecture on thermoresponse and nanoscale assembly.
Main Results:
- Material properties, including thermoresponse and nanoscale assembly, are modulated by the amphiphilic architecture of the hybrid amphiphiles.
- Demonstrated that specific amphiphilic architectures can program protein assembly into adaptive nanoworms.
- Observed a temperature-induced morphological transition from spheres to nanoworms.
Conclusions:
- Judicious design of amphiphilic architecture is key to programming protein self-assembly into functional nanoworms.
- The developed strategy enables the creation of adaptive protein nanomaterials with tunable properties.
- This work advances the field of protein-based biomaterials and their applications.
