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The interactions of ferritins fused with a Ti-recognizing peptide (RKLPDA) and their mutants with titanium oxide substrates were explored with an atomic force microscope (AFM). The amino acid sequence of the peptide was systematically modified to elucidate the role of each amino acid residue in the specific interaction. Force measurements revealed a clear correlation among the sequences in the N-terminal domain of ferritin, surface potentials, and long-range electrostatic interactions. Measurements of adhesion forces clearly revealed that hydrogen bonds take part in the specific binding as well as the electrostatic interaction between charged residues and surface charges of Ti oxides. Moreover, our results indicated that not only the charged and polar residues but also a neutral residue (proline) govern the strength of the specific binding, with the order of the residues also being significant. These results demonstrate that the local structure of the peptide governs the special arrangement of charged residues and strongly affects the strength of the bindings.

Ferritin nanoparticles ornamented with a Ti-binding peptide are versatile nanoscaled building blocks. Their specific binding ability is strong enough to position them on nanopatterned Ti regions on a Pt substrate. Furthermore, the peptides mineralization activity enables the formation of titania on the outer side of the particle, and the particle's inner nanospaces can serve as a carrier for inorganic nanodots. Making use of all these properties, here we show controlled in aqua fabrication of three-dimensional nanoscale structures. The X-Y positioning obeyed the specific binding of the peptide, while fabrication in the Z-dimension entailed stepwise formation of titania and ferritin layers by alternately applying the binding and mineralization abilities of the Ti-binding peptide. This method paves the way for in aqua fabrication of nanodevices having complicated structures and functions.

A two-dimensional hexagonally close-packed (2D-HCP) array of ferritin molecules with a nanoparticle core was fabricated directly on a carbonaceous solid substrate by genetically modifying the outer surface of the ferritin with carbonaceous materials-specific binding peptides. The displayed peptides endowed ferritins with a specific protein-substrate interaction and masked the strong nonspecific interaction. The specific interaction was weak enough to allow ferritins to be rearranged as well as an attractive protein-protein interaction that could be adjusted by selecting the buffer conditions. This method not only produced 2D-HCP arrays of ferritin but also 2D-ordered arrays of independent inorganic nanoparticles after protein elimination that can be applied to floating gate memories.