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    Area of Science:

    • Materials Science
    • Nanotechnology
    • Biotechnology

    Background:

    • Proteins offer complex nanoscale building blocks with diverse functions and structures.
    • Synthetically engineering protein-based materials is challenging due to complex protein surface interactions.
    • Existing synthetic nanoparticles have limitations in design space and complexity.

    Purpose of the Study:

    • To develop a method for controlling protein self-assembly into well-defined materials and crystals.
    • To leverage programmable DNA-DNA interactions to replace complex protein-protein interactions.
    • To explore the design space of protein-DNA conjugates for novel nanomaterial architectures.

    Main Methods:

    • Surface modification of proteins with DNA to create protein-DNA conjugates.
    • Tuning assembly behavior by controlling DNA sequence, protein sequence, and DNA attachment chemistry/position.
    • Designing directional interactions and valency on protein surfaces through mutagenesis and DNA modification.

    Main Results:

    • Demonstrated control over protein monomer energy barriers via oligonucleotide properties.
    • Achieved directional binding and one-dimensional assembly using bivalent protein-DNA building blocks.
    • Successfully assembled densely DNA-modified proteins into crystalline superlattices, similar to DNA-functionalized nanoparticles.
    • Showcased unique crystallization pathways and exotic structures by controlling DNA spatial distribution on proteins.

    Conclusions:

    • Protein-DNA conjugates provide a powerful platform for programmable nanomaterial assembly.
    • This approach expands the design space beyond inorganic nanoparticles, enabling novel architectures.
    • Further research is needed to establish general design rules for DNA-mediated protein assembly.