Abstract
Binding affinity and specificity are crucial factors that influence nanostructure control by biomineralization peptides. In this paper, we analysed the role that the oligomeric state of a silver biomineralization peptide plays in regulating the morphology of silver nanostructure formation. Oligomerization was achieved by conjugating the silver specific TBP biomineralization peptide to the p53 tetramerization domain peptide (p53Tet). Interestingly, the TBP–p53Tet tetrameric peptide acted as a growth catalyst, controlling silver crystal growth, which resulted in the formation of hexagonal silver nanoplates without consuming the peptide. The TBP–p53Tet peptide caps the surface of the silver crystals, which enhances crystal growth on specific faces and thereby regulates silver nanostructure formation in a catalytic fashion. The present findings not only provide an efficient strategy for controlling silver nanostructure formation by biomineralization peptides, but they also demonstrate that in this case the oligomeric peptides play a unique catalytic role.
Highlights
Inorganic nanomaterials exhibit significantly different properties relative to their bulk-sized counterparts
In order to regulate the oligomeric state of a biomineralization peptide, the silver binding through conjugating a biomineralization peptide (TBP) peptide[25] was fused to the tetramerization domain of p53(p53Tet) to produce the TBP–p53Tet peptide
We have demonstrated that oligomerization of the biomineralization peptide enhances their binding specificity towards the surfaces of nanomaterials and the tetrameric biomineralization peptide acted as a silver nanoplate-growth catalyst
Summary
Inorganic nanomaterials exhibit significantly different properties relative to their bulk-sized counterparts. A number of biomineralization peptides have been identified and used to prepare a wide variety of functional inorganic nanomaterials[15,16,17] Some of these biomineralization peptides have been shown to bind to a specific crystal plane, and thereby control nanocrystal shape by directing a colloidal nanocrystal synthetic process[18]. We demonstrated that controlling the precise topological assignment of a palladium biomineralization peptide results in enhanced catalytic activity of the nanomaterial[22] In this case, the oligomeric state of the biomineralization peptide was varied using the tetramerization domain of the tumour suppressor protein p53 (p53Tet) as the control element[23, 24]. The results suggest that the effect of oligomerization on biomineralization peptides can vary tremendously depending on the type of metal ion used during the nanoplate formation process
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