Oligomerization enhances the binding affinity of a silver biomineralization peptide and catalyzes nanostructure formation
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....
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Nature Portfolio
2017
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oai:doaj.org-article:4b9a0866a5ec48389331095e79a3f9b12021-12-02T16:06:32ZOligomerization enhances the binding affinity of a silver biomineralization peptide and catalyzes nanostructure formation10.1038/s41598-017-01442-82045-2322https://doaj.org/article/4b9a0866a5ec48389331095e79a3f9b12017-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-01442-8https://doaj.org/toc/2045-2322Abstract 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.Tatsuya SakaguchiJose Isagani B. JanairoMathieu Lussier-PriceJunya WadaJames G. OmichinskiKazuyasu SakaguchiNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-10 (2017) |
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Medicine R Science Q Tatsuya Sakaguchi Jose Isagani B. Janairo Mathieu Lussier-Price Junya Wada James G. Omichinski Kazuyasu Sakaguchi Oligomerization enhances the binding affinity of a silver biomineralization peptide and catalyzes nanostructure formation |
| description |
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. |
| format |
article |
| author |
Tatsuya Sakaguchi Jose Isagani B. Janairo Mathieu Lussier-Price Junya Wada James G. Omichinski Kazuyasu Sakaguchi |
| author_facet |
Tatsuya Sakaguchi Jose Isagani B. Janairo Mathieu Lussier-Price Junya Wada James G. Omichinski Kazuyasu Sakaguchi |
| author_sort |
Tatsuya Sakaguchi |
| title |
Oligomerization enhances the binding affinity of a silver biomineralization peptide and catalyzes nanostructure formation |
| title_short |
Oligomerization enhances the binding affinity of a silver biomineralization peptide and catalyzes nanostructure formation |
| title_full |
Oligomerization enhances the binding affinity of a silver biomineralization peptide and catalyzes nanostructure formation |
| title_fullStr |
Oligomerization enhances the binding affinity of a silver biomineralization peptide and catalyzes nanostructure formation |
| title_full_unstemmed |
Oligomerization enhances the binding affinity of a silver biomineralization peptide and catalyzes nanostructure formation |
| title_sort |
oligomerization enhances the binding affinity of a silver biomineralization peptide and catalyzes nanostructure formation |
| publisher |
Nature Portfolio |
| publishDate |
2017 |
| url |
https://doaj.org/article/4b9a0866a5ec48389331095e79a3f9b1 |
| work_keys_str_mv |
AT tatsuyasakaguchi oligomerizationenhancesthebindingaffinityofasilverbiomineralizationpeptideandcatalyzesnanostructureformation AT joseisaganibjanairo oligomerizationenhancesthebindingaffinityofasilverbiomineralizationpeptideandcatalyzesnanostructureformation AT mathieulussierprice oligomerizationenhancesthebindingaffinityofasilverbiomineralizationpeptideandcatalyzesnanostructureformation AT junyawada oligomerizationenhancesthebindingaffinityofasilverbiomineralizationpeptideandcatalyzesnanostructureformation AT jamesgomichinski oligomerizationenhancesthebindingaffinityofasilverbiomineralizationpeptideandcatalyzesnanostructureformation AT kazuyasusakaguchi oligomerizationenhancesthebindingaffinityofasilverbiomineralizationpeptideandcatalyzesnanostructureformation |
| _version_ |
1718384958176755712 |