DNA-mediated engineering of multicomponent enzyme crystals.

Area of Science:

• Nanotechnology
• Materials Science
• Biomolecular Engineering

Background:

• Controlling the coassembly of diverse nanoscale building blocks (e.g., biomolecules and nanoparticles) is crucial for applications in catalysis, sensing, and photonics.
• Engineering specific interparticle contacts, particularly with complex biomolecules like proteins, remains a significant challenge.

Purpose of the Study:

• To develop a generalizable strategy for directing the self-assembly of functionalized proteins and nanoparticles into ordered crystalline structures.
• To leverage programmable DNA-DNA interactions to precisely control the assembly process and material properties.

Main Methods:

• Functionalizing two proteins with distinct surface chemistries with nucleic acids.
• Utilizing DNA-DNA hybridization to mediate the coassembly of these proteins, or proteins and DNA-modified gold nanoparticles.
• Characterizing the resulting crystalline lattices for symmetry, composition, and habit.

Main Results:

• Successfully directed the assembly of six unique lattices using catalytically active proteins, or a combination of proteins and gold nanoparticles.
• Demonstrated precise control over lattice symmetries, unit cell constants, and crystal habit through programmable DNA interactions.
• Created novel crystalline materials by exploiting the diverse properties of proteins.

Conclusions:

• The developed strategy offers a generalizable approach for constructing advanced crystalline materials by precisely controlling protein-DNA interactions.
• This method enables the integration of protein functionalities into ordered nanomaterials, opening avenues for catalysis, sensing, and photonics.
• The programmable nature of DNA interactions provides a powerful tool for designing complex, functional nanoscale architectures.