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Hydroxyapatite Formation Coexists with Amyloid-like Self-Assembly of Human Amelogenin

Tooth enamel is formed in an extracellular environment. Amelogenin, the major component in the protein matrix of tooth enamel during the developing stage, could assemble into high molecular weight structures, regulating enamel formation. However, the molecular structure of amelogenin protein assembl...

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Detalles Bibliográficos
Autores principales: Zhang, Jing, Wang, Jian, Ma, Chengwei, Lu, Junxia
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7216246/
https://www.ncbi.nlm.nih.gov/pubmed/32331340
http://dx.doi.org/10.3390/ijms21082946
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author Zhang, Jing
Wang, Jian
Ma, Chengwei
Lu, Junxia
author_facet Zhang, Jing
Wang, Jian
Ma, Chengwei
Lu, Junxia
author_sort Zhang, Jing
collection PubMed
description Tooth enamel is formed in an extracellular environment. Amelogenin, the major component in the protein matrix of tooth enamel during the developing stage, could assemble into high molecular weight structures, regulating enamel formation. However, the molecular structure of amelogenin protein assembly at the functional state is still elusive. In this work, we found that amelogenin is able to induce calcium phosphate minerals into hydroxyapatite (HAP) structure in vitro at pH 6.0. Assessed using X-ray diffraction (XRD) and (31)P solid-state NMR (SSNMR) evidence, the formed HAP mimics natural enamel closely. The structure of amelogenin protein assembly coexisting with the HAP was also studied using atomic force microscopy (AFM), transmission electron microscopy (TEM) and XRD, indicating the β-amyloid structure of the protein. SSNMR was proven to be an important tool in detecting both the rigid and dynamic components of the protein assembly in the sample, and the core sequence (18)EVLTPLKWYQSI(29) was identified as the major segment contributing to the β-sheet secondary structure. Our research suggests an amyloid structure may be an important factor in controlling HAP formation at the right pH conditions with the help of other structural components in the protein assembly.
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spelling pubmed-72162462020-05-22 Hydroxyapatite Formation Coexists with Amyloid-like Self-Assembly of Human Amelogenin Zhang, Jing Wang, Jian Ma, Chengwei Lu, Junxia Int J Mol Sci Article Tooth enamel is formed in an extracellular environment. Amelogenin, the major component in the protein matrix of tooth enamel during the developing stage, could assemble into high molecular weight structures, regulating enamel formation. However, the molecular structure of amelogenin protein assembly at the functional state is still elusive. In this work, we found that amelogenin is able to induce calcium phosphate minerals into hydroxyapatite (HAP) structure in vitro at pH 6.0. Assessed using X-ray diffraction (XRD) and (31)P solid-state NMR (SSNMR) evidence, the formed HAP mimics natural enamel closely. The structure of amelogenin protein assembly coexisting with the HAP was also studied using atomic force microscopy (AFM), transmission electron microscopy (TEM) and XRD, indicating the β-amyloid structure of the protein. SSNMR was proven to be an important tool in detecting both the rigid and dynamic components of the protein assembly in the sample, and the core sequence (18)EVLTPLKWYQSI(29) was identified as the major segment contributing to the β-sheet secondary structure. Our research suggests an amyloid structure may be an important factor in controlling HAP formation at the right pH conditions with the help of other structural components in the protein assembly. MDPI 2020-04-22 /pmc/articles/PMC7216246/ /pubmed/32331340 http://dx.doi.org/10.3390/ijms21082946 Text en © 2020 by the authors. 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 (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Zhang, Jing
Wang, Jian
Ma, Chengwei
Lu, Junxia
Hydroxyapatite Formation Coexists with Amyloid-like Self-Assembly of Human Amelogenin
title Hydroxyapatite Formation Coexists with Amyloid-like Self-Assembly of Human Amelogenin
title_full Hydroxyapatite Formation Coexists with Amyloid-like Self-Assembly of Human Amelogenin
title_fullStr Hydroxyapatite Formation Coexists with Amyloid-like Self-Assembly of Human Amelogenin
title_full_unstemmed Hydroxyapatite Formation Coexists with Amyloid-like Self-Assembly of Human Amelogenin
title_short Hydroxyapatite Formation Coexists with Amyloid-like Self-Assembly of Human Amelogenin
title_sort hydroxyapatite formation coexists with amyloid-like self-assembly of human amelogenin
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7216246/
https://www.ncbi.nlm.nih.gov/pubmed/32331340
http://dx.doi.org/10.3390/ijms21082946
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