Title

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

Disciplines

Biology

Keywords

Amyloid; Biomineralization; Peptides; Nanostructures; Nanowires; Oligomerization; Self-assembly (Chemistry); Tumor suppressor proteins

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