University of Pennsylvania MRSEC Michael L. Klein DMR-0520020

IRGs 3 and 4: Designing Mutations on the Interior Surface of Ferritin-Like Proteins - Jeffery Saven and Ivan Dmochowski

Ferritin proteins are protein assemblies with 4-8 nm interior cavities that provide a versatile, biocompatible platform for the synthesis and encapsulation of oxide and metal nanoparticles. Computational design was used to identify hydrophobic mutations of Dps (up to 120 per dodecamer) consistent with the known structure. The structures and rates of iron mineralization for the mutants are comparable to that of the natural protein

We find that Ferritin-like proteins are robust with respect to designed interior mutations These proteins may provide vehicles for synthesis and improved bioavailability of nanoparticles.

Models of Dps wild type and mutant with 10 designed hydrophobic mutations per subunit.