Determining Peptide Sequence Effects That Control the Size, Structure, and Function of Nanoparticles

Abstract

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.

Thermodynamic Study of Interactions Between ZnO and ZnO Binding Peptides Using Isothermal Titration Calorimetry

“…It has been reported that where peptidepeptide interactions take place forming multilayers, adsorption energies of single peptides can greatly be diminished. 40 Thus, for this system a direct link between thermodynamic changes and the differences observed in morphology modification in the presence of peptides was difficult to obtain. However, ITC allowed direct characterization of ZnO-ZnO-BP interactions and the quantification of energetic changes occurring during the adsorption process.…”

Nanocatalysts for Hiyama, Stille, Kumada, and Negishi C–C Coupling Reactions

“…57 Further investigations have been carried out by the same group in order to identify the structural motifs present in the peptides that actually prevent the nanoparticles from agglomerating, and to fine-tune the size, surface structure, and functionality of single-crystal Pd-NPs between 2 nm and 3 nm using materials directing peptides. 58,59 A special class of compounds that merits separate mention is solvents known as ionic liquids (ILs): ionic compounds that exhibit fluidity at ambient temperatures. 60 ILs can stabilize metal nanoparticles by different mechanisms, intrinsically as well as through the addition of secondary stabilizers.…”

Ultrasensitive Biosensing Platform Based on the Luminescence Quenching Ability of Plasmonic Palladium Nanoparticles

“…Previous reports show that when peptides were used as templates for PdNP fabrication, the amino acids, including histidine, arginine, and asparagine residues, with nitrogen-containing groups in the side chain play an important role in the coordination with Pd. [15] Therefore, we fabricated a polypeptide chain labeled with a fluorescent dye tetramethylrhodamine (TAMRA) as another bioprobe (TAMRA-GLVPRGSNNHHD). The incubation of the dye-labeled peptide (85 nm) with PdNPs resulted in the quenching of TAMRA emission, with the quenching degree dependent on the amount of PdNPs (Figure 4 a).…”