While the morphology of palladium nanoparticles can be favorably manipulated by the presence of amino acid sequences during synthesis, the large scale viability of such an approach has been questioned due to the cost associated with the peptide or protein included in the reduction step. A more appropriate question which addresses the underlying issues with the peptide / protein is how pure must it be to be effective in bio-templating. Crude lysate, desalted lysate, and ion exchange fractions containing a recombinant fusion protein consisting of three copies of a metal binding sequence (Pd4) with Green Fluorescent Protein (GFP) served as sources of material to test the following hypothesis, high purity (Pd4)3GFP may not be necessary to dictate nanoparticle synthesis. Nanoparticles on the order of (2 nm) were prepared under a variety of conditions, and characterized using several methods (transmission electron microscopy (TEM), UV-visible spectroscopy, energy-dispersive X-ray spectroscopy, and high resolution TEM). This presentation will present our findings that indicate palladium nanoparticles can be synthesized without extensive purification of (Pd4)3-GFP, indicating that a recombinant approach to produce Pd4 appears to be a highly attractive from both a scientific and economic standpoint.

Effect of peptide/protein purity on bio-templated nanoparticle synthesis: Morphologies, properties, and ultimate cost

256th National Meeting (2018)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.