Abstract
Aptamers with 12 amino acid peptides that specifically bind to silicon dioxide (SiO2) were obtained through the phage-display method. A quartz crystal microbalance (QCM) measurement showed that the peptides bound to the SiO2 surface quickly, and that the lowest dissociation constant (Kd) was 16 micromolars (mM). The recombinant ferritins, cage-shaped protein mutants that had the aptamers on their outer surface, showed a much higher binding affinity to the SiO2 surface, and the Kd reached as low as 2.3 nm. The results indicated that multiple aptamers coordinately bound to the SiO2 surface. It was demonstrated that the aptamers on the outer surface had the ability to selectively deliver the recombinant ferritins with a nanoparticle (NP) to the SiO2 surface. The NP array made by the recombinant ferritin on the SiO2 substrate could be used as a nanoetching mask. This technique for making an NP array through ferritins is being applied to other cage-shaped proteins.
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