Uniaxial Hydroxyapatite Growth on a Self-Assembled Protein Scaffold

Biomineralization is a crucial process whereby organisms produce mineralized tissues such as teeth for mastication, bones for support, and shells for protection. Mineralized tissues are composed of hierarchically organized hydroxyapatite crystals, with a limited capacity to regenerate when demineral...

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Autores principales:	Alexander L. Danesi, Dimitra Athanasiadou, Ahmad Mansouri, Alina Phen, Mehrnoosh Neshatian, James Holcroft, Johan Bonde, Bernhard Ganss, Karina M. M. Carneiro
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	biomineralization biomimetics bio-inspired materials amelogenin amelotin hydroxyapatite enamel Biology (General) QH301-705.5 Chemistry QD1-999
Acceso en línea:	https://doaj.org/article/4eb15481eda040389406a6a493bd6502
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spelling	oai:doaj.org-article:4eb15481eda040389406a6a493bd65022021-11-25T17:55:34ZUniaxial Hydroxyapatite Growth on a Self-Assembled Protein Scaffold10.3390/ijms2222123431422-00671661-6596https://doaj.org/article/4eb15481eda040389406a6a493bd65022021-11-01T00:00:00Zhttps://www.mdpi.com/1422-0067/22/22/12343https://doaj.org/toc/1661-6596https://doaj.org/toc/1422-0067Biomineralization is a crucial process whereby organisms produce mineralized tissues such as teeth for mastication, bones for support, and shells for protection. Mineralized tissues are composed of hierarchically organized hydroxyapatite crystals, with a limited capacity to regenerate when demineralized or damaged past a critical size. Thus, the development of protein-based materials that act as artificial scaffolds to guide hydroxyapatite growth is an attractive goal both for the design of ordered nanomaterials and for tissue regeneration. In particular, amelogenin, which is the main protein that scaffolds the hierarchical organization of hydroxyapatite crystals in enamel, amelogenin recombinamers, and amelogenin-derived peptide scaffolds have all been investigated for in vitro mineral growth. Here, we describe uniaxial hydroxyapatite growth on a nanoengineered amelogenin scaffold in combination with amelotin, a mineral promoting protein present during enamel formation. This bio-inspired approach for hydroxyapatite growth may inform the molecular mechanism of hydroxyapatite formation in vitro as well as possible mechanisms at play during mineralized tissue formation.Alexander L. DanesiDimitra AthanasiadouAhmad MansouriAlina PhenMehrnoosh NeshatianJames HolcroftJohan BondeBernhard GanssKarina M. M. CarneiroMDPI AGarticlebiomineralizationbiomimeticsbio-inspired materialsamelogeninamelotin hydroxyapatiteenamelBiology (General)QH301-705.5ChemistryQD1-999ENInternational Journal of Molecular Sciences, Vol 22, Iss 12343, p 12343 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	biomineralization biomimetics bio-inspired materials amelogenin amelotin hydroxyapatite enamel Biology (General) QH301-705.5 Chemistry QD1-999
spellingShingle	biomineralization biomimetics bio-inspired materials amelogenin amelotin hydroxyapatite enamel Biology (General) QH301-705.5 Chemistry QD1-999 Alexander L. Danesi Dimitra Athanasiadou Ahmad Mansouri Alina Phen Mehrnoosh Neshatian James Holcroft Johan Bonde Bernhard Ganss Karina M. M. Carneiro Uniaxial Hydroxyapatite Growth on a Self-Assembled Protein Scaffold
description	Biomineralization is a crucial process whereby organisms produce mineralized tissues such as teeth for mastication, bones for support, and shells for protection. Mineralized tissues are composed of hierarchically organized hydroxyapatite crystals, with a limited capacity to regenerate when demineralized or damaged past a critical size. Thus, the development of protein-based materials that act as artificial scaffolds to guide hydroxyapatite growth is an attractive goal both for the design of ordered nanomaterials and for tissue regeneration. In particular, amelogenin, which is the main protein that scaffolds the hierarchical organization of hydroxyapatite crystals in enamel, amelogenin recombinamers, and amelogenin-derived peptide scaffolds have all been investigated for in vitro mineral growth. Here, we describe uniaxial hydroxyapatite growth on a nanoengineered amelogenin scaffold in combination with amelotin, a mineral promoting protein present during enamel formation. This bio-inspired approach for hydroxyapatite growth may inform the molecular mechanism of hydroxyapatite formation in vitro as well as possible mechanisms at play during mineralized tissue formation.
format	article
author	Alexander L. Danesi Dimitra Athanasiadou Ahmad Mansouri Alina Phen Mehrnoosh Neshatian James Holcroft Johan Bonde Bernhard Ganss Karina M. M. Carneiro
author_facet	Alexander L. Danesi Dimitra Athanasiadou Ahmad Mansouri Alina Phen Mehrnoosh Neshatian James Holcroft Johan Bonde Bernhard Ganss Karina M. M. Carneiro
author_sort	Alexander L. Danesi
title	Uniaxial Hydroxyapatite Growth on a Self-Assembled Protein Scaffold
title_short	Uniaxial Hydroxyapatite Growth on a Self-Assembled Protein Scaffold
title_full	Uniaxial Hydroxyapatite Growth on a Self-Assembled Protein Scaffold
title_fullStr	Uniaxial Hydroxyapatite Growth on a Self-Assembled Protein Scaffold
title_full_unstemmed	Uniaxial Hydroxyapatite Growth on a Self-Assembled Protein Scaffold
title_sort	uniaxial hydroxyapatite growth on a self-assembled protein scaffold
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/4eb15481eda040389406a6a493bd6502
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Uniaxial Hydroxyapatite Growth on a Self-Assembled Protein Scaffold

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