Journal
ACS NANO
Volume 8, Issue 9, Pages 9097-9106Publisher
AMER CHEMICAL SOC
DOI: 10.1021/nn502551y
Keywords
recombinant iron-binding protein; protein-mediated particle nucleation; in situ TEM analysis
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Funding
- Department of Energy, Office of Science, Early Career Research Award, Biomolecular Materials Program
- U.S. Department of Energy, Office of Basic Energy Science, Division of Materials Sciences and Engineering
- US. Department of Energy by Iowa State University [DE-AC02-07CH11358]
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Biomineralization proteins are widely used as templating agents in biomimetic synthesis of a variety of organic-inorganic nanostructures. However, the role of the protein in controlling the nucleation and growth of biomimetic particles is not well understood, because the mechanism of the bioinspired reaction is often deduced from at situ analysis of the resultant nanoscale mineral phase. Here we report the direct visualization of biomimetic iron oxide nanoparticle nucleation mediated by an acidic bacterial recombinant protein, Mms6, during an in situ reaction induced by the controlled addition of sodium hydroxide to solution-phase Mms6 protein micelles incubated with ferric chloride. Using in situ liquid cell scanning transmission electron microscopy we observe the liquid iron prenucleation phase and nascent amorphous nanoparticles forming preferentially on the surface of protein micelles. Our results provide insight into the early steps of protein-mediated biomimetic nucleation of iron oxide and point to the importance of an extended protein surface during nanoparticle formation.
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