Synergic strategies for the enhanced self-assembly of biomineralization peptides for the synthesis of functional nanomaterials
College
College of Science
Department/Unit
Biology
Document Type
Article
Source Title
Protein and Peptide Letters
Volume
25
Issue
1
First Page
4
Last Page
14
Publication Date
1-1-2018
Abstract
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.
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Digitial Object Identifier (DOI)
10.2174/0929866525666171214110206
Recommended Citation
Janairo, J. B., Sakaguchi, T., Mine, K., Kamada, R., & Sakaguchi, K. (2018). Synergic strategies for the enhanced self-assembly of biomineralization peptides for the synthesis of functional nanomaterials. Protein and Peptide Letters, 25 (1), 4-14. https://doi.org/10.2174/0929866525666171214110206
Disciplines
Biology
Keywords
Amyloid; Biomineralization; Peptides; Nanostructures; Nanowires; Oligomerization; Self-assembly (Chemistry); Tumor suppressor proteins
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