Biomineralization through a Symmetry-Controlled Oligomeric Peptide
Biomineralization peptides are versatile tools for generating nanostructures since they can make specific interactions with various inorganic metals, which can lead to the formation of intricate nanostructures. Previously, we examined the influence that multivalency has on inorganic structures forme...
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| Format: | Article |
| Language: | English |
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MDPI AG
2023-12-01
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| Series: | Biomimetics |
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| Online Access: | https://www.mdpi.com/2313-7673/8/8/606 |
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| author | Tatsuya Sakaguchi Natsumi Nakagawa Kenta Mine Jose Isagani B. Janairo Rui Kamada James G. Omichinski Kazuyasu Sakaguchi |
| author_facet | Tatsuya Sakaguchi Natsumi Nakagawa Kenta Mine Jose Isagani B. Janairo Rui Kamada James G. Omichinski Kazuyasu Sakaguchi |
| author_sort | Tatsuya Sakaguchi |
| collection | DOAJ |
| description | Biomineralization peptides are versatile tools for generating nanostructures since they can make specific interactions with various inorganic metals, which can lead to the formation of intricate nanostructures. Previously, we examined the influence that multivalency has on inorganic structures formed by p53 tetramer-based biomineralization peptides and noted a connection between the geometry of the peptide and its ability to regulate nanostructure formation. To investigate the role of multivalency in nanostructure formation by biomineralization peptides more thoroughly, silver biomineralization peptides were engineered by linking them to additional self-assembling molecules based on coiled-coil peptides and multistranded DNA oligomers. Under mild reducing conditions at room temperature, these engineered biomineralization peptides self-assembled and formed silver nanostructures. The trimeric forms of the biomineralization peptides were the most efficient in forming a hexagonal disk nanostructure, with both the coiled-coil peptide and DNA-based multimeric forms. Together, the results suggest that the spatial arrangement of biomineralization peptides plays a more important role in regulating nanostructure formation than their valency. |
| first_indexed | 2024-03-08T20:57:21Z |
| format | Article |
| id | doaj.art-03f66d2cfb8a450585936c9dec4bcaeb |
| institution | Directory Open Access Journal |
| issn | 2313-7673 |
| language | English |
| last_indexed | 2024-03-08T20:57:21Z |
| publishDate | 2023-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomimetics |
| spelling | doaj.art-03f66d2cfb8a450585936c9dec4bcaeb2023-12-22T13:55:39ZengMDPI AGBiomimetics2313-76732023-12-018860610.3390/biomimetics8080606Biomineralization through a Symmetry-Controlled Oligomeric PeptideTatsuya Sakaguchi0Natsumi Nakagawa1Kenta Mine2Jose Isagani B. Janairo3Rui Kamada4James G. Omichinski5Kazuyasu Sakaguchi6Laboratory of Biological Chemistry, Department of Chemistry, Faculty of Science, Hokkaido University, Sapporo 060-0810, JapanLaboratory of Biological Chemistry, Department of Chemistry, Faculty of Science, Hokkaido University, Sapporo 060-0810, JapanLaboratory of Biological Chemistry, Department of Chemistry, Faculty of Science, Hokkaido University, Sapporo 060-0810, JapanBiology Department, De La Salle University, 2401 Taft Avenue, Manila 0922, PhilippinesLaboratory of Biological Chemistry, Department of Chemistry, Faculty of Science, Hokkaido University, Sapporo 060-0810, JapanDépartement de Biochimie et Médicine Moléculaire, Université de Montréal, Montréal, QC H3C 3J7, CanadaLaboratory of Biological Chemistry, Department of Chemistry, Faculty of Science, Hokkaido University, Sapporo 060-0810, JapanBiomineralization peptides are versatile tools for generating nanostructures since they can make specific interactions with various inorganic metals, which can lead to the formation of intricate nanostructures. Previously, we examined the influence that multivalency has on inorganic structures formed by p53 tetramer-based biomineralization peptides and noted a connection between the geometry of the peptide and its ability to regulate nanostructure formation. To investigate the role of multivalency in nanostructure formation by biomineralization peptides more thoroughly, silver biomineralization peptides were engineered by linking them to additional self-assembling molecules based on coiled-coil peptides and multistranded DNA oligomers. Under mild reducing conditions at room temperature, these engineered biomineralization peptides self-assembled and formed silver nanostructures. The trimeric forms of the biomineralization peptides were the most efficient in forming a hexagonal disk nanostructure, with both the coiled-coil peptide and DNA-based multimeric forms. Together, the results suggest that the spatial arrangement of biomineralization peptides plays a more important role in regulating nanostructure formation than their valency.https://www.mdpi.com/2313-7673/8/8/606biomineralization peptidesilver nanostructurecoiled-coil peptidesDNA-based scaffoldhexagonal disk |
| spellingShingle | Tatsuya Sakaguchi Natsumi Nakagawa Kenta Mine Jose Isagani B. Janairo Rui Kamada James G. Omichinski Kazuyasu Sakaguchi Biomineralization through a Symmetry-Controlled Oligomeric Peptide Biomimetics biomineralization peptide silver nanostructure coiled-coil peptides DNA-based scaffold hexagonal disk |
| title | Biomineralization through a Symmetry-Controlled Oligomeric Peptide |
| title_full | Biomineralization through a Symmetry-Controlled Oligomeric Peptide |
| title_fullStr | Biomineralization through a Symmetry-Controlled Oligomeric Peptide |
| title_full_unstemmed | Biomineralization through a Symmetry-Controlled Oligomeric Peptide |
| title_short | Biomineralization through a Symmetry-Controlled Oligomeric Peptide |
| title_sort | biomineralization through a symmetry controlled oligomeric peptide |
| topic | biomineralization peptide silver nanostructure coiled-coil peptides DNA-based scaffold hexagonal disk |
| url | https://www.mdpi.com/2313-7673/8/8/606 |
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