Journal
CHEMISTRY OF MATERIALS
Volume 23, Issue 17, Pages 3921-3929Publisher
AMER CHEMICAL SOC
DOI: 10.1021/cm201295p
Keywords
composite materials; ferrites; X-ray spectroscopy; pair distribution functions; biomineralization
Funding
- U.S. Department of Energy, Office of Basic Energy Sciences, Division of Materials Science and Engineering [DE-FG02-07ER46477]
- National Science Foundation [CBET-0709358]
- NASA Astrobiology Institute [NNA08CN85A]
- U.S. Department of Energy [DE-AC02-06CH11357, DE-AC02-05CH11231]
- NASA [103836, NNA08CN85A] Funding Source: Federal RePORTER
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Encapsulation of inorganic nanoparticles within oligomeric protein cages can provide a multivalent approach for the synthesis of biocompatible nanomaterials by combining the nanoparticle-forming catalytic abilities of the cage interior with the biointeractive exterior surface of the cage. Protein cages provide more than simply a passive compartment for nanoparticle formation: protein-templated nanopartides can exhibit structural and electronic properties that are dramatically different from materials synthesized without protein templating. Mixed Fe/Mn oxides formed under hydrothermal conditions form a structural series ranging from the gamma-Fe(2)O(3) (maghemite) to the Mn(3)O(4) (hausmannite) spinel structure as the Mn fraction is increased from 0 to 100%, while similar materials formed inside of human ferritin transition instead from maghemite to a layered Mn oxide structure similar to chalcophanite. The electronic properties of the protein-templated nanopartides, as determined from soft X-ray absorption spectroscopy, also differ from those of their protein-free counterparts, in agreement with the structural results. Protein-templated synthesis may provide the opportunity for powerful control over nanomaterial properties through nanoconfinement, but the ultimate physical basis for these effects remains to be determined.
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