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Determining peptide sequence effects that control the size, structure, and function of nanoparticles.

The ability to tune the size, shape, and composition of nanomaterials at length scales <10 nm remains a challenging task. Such capabilities are required to fully realize the application of nanotechnology for catalysis, energy storage, and biomedical technologies. Conversely, nature employs biomacromolecules such as proteins and peptides as highly specific nanoparticle ligands that demonstrate exacting precision over the particle morphology through controlling the biotic/abiotic interface. Here we demonstrate the ability to finely tune the size, surface structure, and functionality of single-crystal Pd nanoparticles between 2 and 3 nm using materials directing peptides. This was achieved by selectively altering the peptide sequence to change the binding motif, which in turn modifies the surface structure of the particles. The materials were fully characterized before and after reduction using atomically resolved spectroscopic and microscopic analyses, which indicated that the coordination environment prior to reduction significantly affects the structure of the final nanoparticles. Additionally, changes to the particle surface structure, as a function of peptide sequence, can allow for chloride ion coordination that alters the catalytic abilities of the materials for the C-C coupling Stille reaction. These results suggest that peptide-based approaches may be able to achieve control over the structure/function relationship of nanomaterials where the peptide sequence could be used to selectivity tune such capabilities.