Genetically Encoded Inverse Bolaamphiphiles

Area of Science:

• Biomaterials Science
• Synthetic Biology
• Nanotechnology

Background:

• Post-translational modifications (PTMs) are crucial for controlling protein function and localization in nature.
• Lipidation, a PTM involving lipid attachment, offers a pathway to engineer protein properties.
• Developing programmable protein-based materials is a key goal in materials science and biotechnology.

Purpose of the Study:

• To synthesize genetically encoded lipidated proteins with controllable hierarchical assembly.
• To leverage orthogonal lipidation pathways for precise control over protein modification.
• To create novel recombinant nanomaterials with tunable structures and morphologies.

Main Methods:

• Utilized two orthogonal lipidation pathways (N-myristoylation and C-cholesterylation) within *Escherichia coli*.
• Engineered recombinant proteins with distinct lipidation domains at each terminus.
• Investigated the self-assembly behavior of the resulting triblock architecture (inverse bolaamphiphiles).

Main Results:

• Demonstrated the successful orthogonality of N-myristoylation and C-cholesterylation pathways.
• Produced recombinant lipidated proteins with a defined triblock architecture.
• Showed that protein architecture and polypeptide sequence dictate hierarchical self-assembly.

Conclusions:

• The bio-enabled approach allows for the creation of novel recombinant hybrid biomaterials.
• Tunable nanoscale structures and morphologies can be achieved through controlled lipidation.
• This method holds potential for applications in nanobiotechnology and advanced materials development.