Protein-assisted synthesis route of metal nanoparticles: exploration of key chemistry of the biomolecule

Essentially, biomolecule assisted synthesis of inorganic nanoparticles can be divided into two categories. One uses multi-domain protein cages (template) and other relies on the self-assembly of the biomolecules including small peptides, DNA, and denatured protein. Protein templated synthesis of various nanomaterials is relatively well understood as the cages of the biological macromolecules and their specific interaction with inorganic ions ultimately dictate the size and crystallinity of the nanomaterials. On the other hand formation of nanoparticles using protein in the cost of the native structural integrity for the self-assembly is not well understood till date. In the present work we report a protein-assisted synthesis route to prepare highly crystalline 3–5 nm gold nanoparticles, which relies systematic thermal denaturation of a number of proteins and protein mixture from Escherichia coli in absence of any reducing agent. By using UV–vis, circular dichroism spectroscopy, and high-resolution transmission electron microscopy we have explored details of the associated biochemistry of the proteins dictating kinetics, size, and crystallinity of the nanoparticles. The kinetics of nanoparticles formation in this route, which is sigmoidal in nature, has been modelled in a simple scheme of autocatalytic process. Interestingly, the protein-capped as prepared Au nanoparticles are found to serve as effective catalyst to activate the reduction of 4-nitrophenol in the presence of NaBH4. The kinetic data obtained by monitoring the reduction of 4-nitrophenol by UV/vis-spectroscopy revealing the efficient catalytic activity of the nanoparticles have been explained in terms of the Langmuir–Hinshelwood model. The methodology and the details of the protein chemistry presented here may find relevance in the protein-assisted synthesis of inorganic nanostructures in general.