Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Danesi, Alexander L., Athanasiadou, Dimitra, Mansouri, Ahmad, Phen, Alina, Neshatian, Mehrnoosh, Holcroft, James, Bonde, Johan, Ganss, Bernhard, Carneiro, Karina M. M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8620880/
https://www.ncbi.nlm.nih.gov/pubmed/34830225
http://dx.doi.org/10.3390/ijms222212343
_version_ 1784605325082492928
author Danesi, Alexander L.
Athanasiadou, Dimitra
Mansouri, Ahmad
Phen, Alina
Neshatian, Mehrnoosh
Holcroft, James
Bonde, Johan
Ganss, Bernhard
Carneiro, Karina M. M.
author_facet Danesi, Alexander L.
Athanasiadou, Dimitra
Mansouri, Ahmad
Phen, Alina
Neshatian, Mehrnoosh
Holcroft, James
Bonde, Johan
Ganss, Bernhard
Carneiro, Karina M. M.
author_sort Danesi, Alexander L.
collection PubMed
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 Online
Article
Text
id pubmed-8620880
institution National Center for Biotechnology Information
language English
publishDate 2021
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-86208802021-11-27 Uniaxial Hydroxyapatite Growth on a Self-Assembled Protein Scaffold Danesi, Alexander L. Athanasiadou, Dimitra Mansouri, Ahmad Phen, Alina Neshatian, Mehrnoosh Holcroft, James Bonde, Johan Ganss, Bernhard Carneiro, Karina M. M. Int J Mol Sci Article 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. MDPI 2021-11-15 /pmc/articles/PMC8620880/ /pubmed/34830225 http://dx.doi.org/10.3390/ijms222212343 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Danesi, Alexander L.
Athanasiadou, Dimitra
Mansouri, Ahmad
Phen, Alina
Neshatian, Mehrnoosh
Holcroft, James
Bonde, Johan
Ganss, Bernhard
Carneiro, Karina M. M.
Uniaxial Hydroxyapatite Growth on a Self-Assembled Protein Scaffold
title 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_short Uniaxial Hydroxyapatite Growth on a Self-Assembled Protein Scaffold
title_sort uniaxial hydroxyapatite growth on a self-assembled protein scaffold
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8620880/
https://www.ncbi.nlm.nih.gov/pubmed/34830225
http://dx.doi.org/10.3390/ijms222212343
work_keys_str_mv AT danesialexanderl uniaxialhydroxyapatitegrowthonaselfassembledproteinscaffold
AT athanasiadoudimitra uniaxialhydroxyapatitegrowthonaselfassembledproteinscaffold
AT mansouriahmad uniaxialhydroxyapatitegrowthonaselfassembledproteinscaffold
AT phenalina uniaxialhydroxyapatitegrowthonaselfassembledproteinscaffold
AT neshatianmehrnoosh uniaxialhydroxyapatitegrowthonaselfassembledproteinscaffold
AT holcroftjames uniaxialhydroxyapatitegrowthonaselfassembledproteinscaffold
AT bondejohan uniaxialhydroxyapatitegrowthonaselfassembledproteinscaffold
AT ganssbernhard uniaxialhydroxyapatitegrowthonaselfassembledproteinscaffold
AT carneirokarinamm uniaxialhydroxyapatitegrowthonaselfassembledproteinscaffold