In Aqua Manufacturing of a Three-Dimensional Nanostructure Using a Peptide Aptamer
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Manufacturing of a Three-Dimensional Nanostructure Using a Peptide Aptamer Ken-Ichi Sano and Kiyotaka Shiba
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 threedimensional (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.
Introduction Biomolecules excel at specific, or selective, recognition of other molecules. The various combinations of 20 amino acids provide polypeptides with the ability to distinguish particular target molecules from others. What’s more, developments in molecular evolutionary methodology have enabled us to create artificial peptides that specifically bind to selected target molecules assigned by researchers.1 This technique was originally established to evolve peptides that would bind to biomolecular targets such as receptors and enzymes. Over the years, however, the targets have been extended to inorganic molecules.2,3 Specific peptide binders, also called aptamers, have been created that recognize a variety of materials.4,5 524
With these material-binding peptides, we can endow the surfaces of target materials with the specific binding ability of these peptides. Possible usages of the nanomaterials having targeting ability in the fields of materials sciences and medical applications were reviewed elsewhere.4, 5 Using our titanium (Ti) binding peptide, TBP-1, as a model, we will show here how such material-binding peptides can be used for bottom-up in aqua nanofabrication.
selected for its capacity to bind to Ti particles through a biopanning process using a commercially available peptide phage system.6 Because the surface structure of an inorganic material such as Ti is rather monotonous compared to that of a biomacromolecule, we were interested in finding out how TBP-1 recogni
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