Abstract

Proteins and peptides have attracted much attention as templates for one-pot synthesis of biocompatible gold nanoparticles. While numerous natural and de novo protein sequences have been used, the actual mechanism of nanoparticle nucleation and growth from the protein matrix is not well understood. In this study we utilized engineered consensus tetratricopeptide repeat protein (CTPR) to probe the bioinorganic interface during gold nanoparticle synthesis. The binding of CTPR to gold ions and the gold nanoparticle surface was investigated using fluorescence spectroscopy and heteronuclear single quantum coherence NMR spectroscopy to provide residue-specific measurements. This work provides a foundation for the rational design of proteins for synthesis of tailored functional nanomaterials for biological, medical, and optical applications.

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