Synergic strategies for the enhanced self-assembly of biomineralization peptides for the synthesis of functional nanomaterials

Introduction: Peptide-mediated biomineralization is a promising bioinspired technique of nanostructure formation. The biomineralization peptide is responsible for the regulation of the growth and morphology of the inorganic nanostructure. The 3D properties of the biomineralization peptide is a cruci...

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Main Authors: Janairo, Jose Isagani B., Sakaguchi, Tatsuya, Mine, Kenta, Kamada, Rui, Sakaguchi, Kazuyasu
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Published: Animo Repository 2018
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https://animorepository.dlsu.edu.ph/context/faculty_research/article/2637/type/native/viewcontent
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spelling oai:animorepository.dlsu.edu.ph:faculty_research-26372021-07-08T06:54:48Z Synergic strategies for the enhanced self-assembly of biomineralization peptides for the synthesis of functional nanomaterials Janairo, Jose Isagani B. Sakaguchi, Tatsuya Mine, Kenta Kamada, Rui Sakaguchi, Kazuyasu Introduction: Peptide-mediated biomineralization is a promising bioinspired technique of nanostructure formation. The biomineralization peptide is responsible for the regulation of the growth and morphology of the inorganic nanostructure. The 3D properties of the biomineralization peptide is a crucial factor in which the success of creating functional nanomaterials depends on. However, given the relatively short sequence of most biomineralization peptides, controlling the multivalency and spatial orientation of the peptide can be a challenging endeavor. Objective: This mini-review details recent advances in enhancing the self-assembly and 3D properties of the biomineralization peptide. The design and creation of fusion peptides is highlighted, which involves the conjugation of the biomineralization peptide with a control element. The control element is responsible for directing the self-assembly of the biomineralization peptide. Conclusion: A variety of control elements that can direct the self-assembly of biomineralization peptides are available. The control element can be a small organic molecule such as a biphenyl, or a peptide segment such as the p53 tetramerization domain or the amyloid peptide. The high diversity of existing control elements further increases the ability of peptide-mediated biomineralization to create functional nanomaterials. © 2018 Bentham Science Publishers. 2018-01-01T08:00:00Z text text/html https://animorepository.dlsu.edu.ph/faculty_research/1638 https://animorepository.dlsu.edu.ph/context/faculty_research/article/2637/type/native/viewcontent Faculty Research Work Animo Repository Amyloid Biomineralization Peptides Nanostructures Nanowires Oligomerization Self-assembly (Chemistry) Tumor suppressor proteins Biology
institution De La Salle University
building De La Salle University Library
continent Asia
country Philippines
Philippines
content_provider De La Salle University Library
collection DLSU Institutional Repository
topic Amyloid
Biomineralization
Peptides
Nanostructures
Nanowires
Oligomerization
Self-assembly (Chemistry)
Tumor suppressor proteins
Biology
spellingShingle Amyloid
Biomineralization
Peptides
Nanostructures
Nanowires
Oligomerization
Self-assembly (Chemistry)
Tumor suppressor proteins
Biology
Janairo, Jose Isagani B.
Sakaguchi, Tatsuya
Mine, Kenta
Kamada, Rui
Sakaguchi, Kazuyasu
Synergic strategies for the enhanced self-assembly of biomineralization peptides for the synthesis of functional nanomaterials
description Introduction: Peptide-mediated biomineralization is a promising bioinspired technique of nanostructure formation. The biomineralization peptide is responsible for the regulation of the growth and morphology of the inorganic nanostructure. The 3D properties of the biomineralization peptide is a crucial factor in which the success of creating functional nanomaterials depends on. However, given the relatively short sequence of most biomineralization peptides, controlling the multivalency and spatial orientation of the peptide can be a challenging endeavor. Objective: This mini-review details recent advances in enhancing the self-assembly and 3D properties of the biomineralization peptide. The design and creation of fusion peptides is highlighted, which involves the conjugation of the biomineralization peptide with a control element. The control element is responsible for directing the self-assembly of the biomineralization peptide. Conclusion: A variety of control elements that can direct the self-assembly of biomineralization peptides are available. The control element can be a small organic molecule such as a biphenyl, or a peptide segment such as the p53 tetramerization domain or the amyloid peptide. The high diversity of existing control elements further increases the ability of peptide-mediated biomineralization to create functional nanomaterials. © 2018 Bentham Science Publishers.
format text
author Janairo, Jose Isagani B.
Sakaguchi, Tatsuya
Mine, Kenta
Kamada, Rui
Sakaguchi, Kazuyasu
author_facet Janairo, Jose Isagani B.
Sakaguchi, Tatsuya
Mine, Kenta
Kamada, Rui
Sakaguchi, Kazuyasu
author_sort Janairo, Jose Isagani B.
title Synergic strategies for the enhanced self-assembly of biomineralization peptides for the synthesis of functional nanomaterials
title_short Synergic strategies for the enhanced self-assembly of biomineralization peptides for the synthesis of functional nanomaterials
title_full Synergic strategies for the enhanced self-assembly of biomineralization peptides for the synthesis of functional nanomaterials
title_fullStr Synergic strategies for the enhanced self-assembly of biomineralization peptides for the synthesis of functional nanomaterials
title_full_unstemmed Synergic strategies for the enhanced self-assembly of biomineralization peptides for the synthesis of functional nanomaterials
title_sort synergic strategies for the enhanced self-assembly of biomineralization peptides for the synthesis of functional nanomaterials
publisher Animo Repository
publishDate 2018
url https://animorepository.dlsu.edu.ph/faculty_research/1638
https://animorepository.dlsu.edu.ph/context/faculty_research/article/2637/type/native/viewcontent
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