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In Aqua Manufacturing of a Three-Dimensional Nanostructure Using a Peptide Aptamer

Published online by Cambridge University Press:  31 January 2011

Ken-Ichi Sano  and
Kiyotaka Shiba
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Abstract

TBP-1 is a 12-amino-acid peptide aptamer that has been isolated as a Ti binder using a peptide-phage system. Subsequent analyses have shown that TBP1 also binds Si and Ag, and has the ability to enhance the formation of titania and silica as well as nanoparticles of Ag. TBP-1 is thus a bifunctional peptide: a binder that also acts as a mediator of mineralization. These two functions can be grafted onto heterologous molecules. For instance, mutational analysis of the TBP-1 revealed that its N -terminal hexapeptide, RKLPDA (minTBP-1), is sufficient for Ti binding. When the surface of ferritin, a nano-sized spherical cargo protein, was ornamented with minTBP-1 either genetically or chemically, the resultant modified ferritin acquired the ability to bind Ti and mediate mineralization. By alternately applying the binding and mineralization activities of the minTBP-1-modified nanocage, we were able to construct, in stepwise fashion, multilayer structures composed of titania (or silica) and nanocages. We named this process the biomimetic layer-by-layer (BioLBL) method. By coupling BioLBL with a conventional top-down lithographic method, in aqua structuralization of a three-dimensional (3D) configuration of nanomolecules was realized. As shown in this article, binding and mineralization activities of peptide aptamers, when they are combined with nanostructured materials, play active roles in manufacturing nanostrucutre in aqua.

Type
Research Article
Information
MRS Bulletin , Volume 33 , Issue 5: Molecular Biomimetics , May 2008 , pp. 524 - 529
Copyright
Copyright © Materials Research Society 2008

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