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Daniel R. Strongin
The iron storage protein, horse spleen ferritin, has been shown to be photoactive for the reduction of Cr(VI) to Cr(III). The protein can be loaded with iron in the laboratory to produce iron oxyhydroxide particles of variable size in the nanoscale regime.
A methodolgy has been developed that uses the biological protein ferritin to assemble supported well defined iron and colbalt based metal oxide and metallic nanoparticles.
As a means to transport photosensitizers to cells horse spleen ferritin has been functionallized with Ru(phen)(bpy)22+. The photoactivation of this complex with visible light leads to a complex that can efficiently convert triplet to singlet oxygen that can potentially be used as an antimicrobial.
Listeria innocua ferritin like protein, has been used to assemble nano colbalt oxide and metallic nanoparticles. This ferritin cloned from bacteria has a smaller cage structure than the more traditionally investigated horse spleen ferritin.