Pierpaolo Ceci

TL;DR: The DNA-binding proteins from starved cells (Dps) are shown to be a Fe-binding and storage protein where Fe(II) oxidation is most effectively accomplished by H2O2 rather than by O2 as in ferritins, and the protective effect of Dps on DNA most likely is exerted through a dual action, the physical association with DNA and the ability to nullify the toxic combination of Fe( II) and H2 O2.

TL;DR: It is shown that electrostatically patchy protein cages--cowpea chlorotic mottle virus and ferritin cages--can be used to direct the self-assembly of three-dimensional binary superlattices, and these magnetic assemblies provide contrast enhancement in magnetic resonance imaging.

TL;DR: The state of the art is that the response to oxidative and peroxide-mediated stress is mediated directly by Dps proteins via their ferritin-like activity.

TL;DR: Dps self-aggregation and Dps-driven DNA condensation are parallel phenomena that reflect the properties of the N-terminus, and DNA protection against the toxic action of Fe(II) and H2O2 is not affected by theN-terminal deletions either in vitro or in vivo.

TL;DR: The investigation of hyperthermic properties of HFt-NPs shows that a Co doping of 5% is enough to strongly enhance the magnetic anisotropy and thus thehyperthermic efficiency with respect to the undoped sample, suggesting this system represents a promising candidate for the development of a protein-based theranostic nanoplatform.