Effect of aspartic acid on the crystallization kinetics of ACP and dentin remineralization
Type I collagen and non-collagen proteins are the main organic components of dentin. This study aimed to investigate the biomimetic remineralization of demineralized dentin by aspartic acid (Asp), which is abundant in non-collagenous proteins (NCPs). Asp was added to a mineralizing solution containi...
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Veröffentlicht in: | Journal of the mechanical behavior of biomedical materials 2021-03, Vol.115, p.104226-104226, Article 104226 |
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container_title | Journal of the mechanical behavior of biomedical materials |
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creator | Zhao, Luyi Sun, Jian Zhang, Ce Chen, Chaoqun Chen, Yi Zheng, Bo Pan, Haihua Shao, Changyu Jin, Biao Tang, Ruikang Gu, Xinhua |
description | Type I collagen and non-collagen proteins are the main organic components of dentin. This study aimed to investigate the biomimetic remineralization of demineralized dentin by aspartic acid (Asp), which is abundant in non-collagenous proteins (NCPs). Asp was added to a mineralizing solution containing polyacrylic acid (PAA) to explore the mechanism of Asp regulating the pure amorphous calcium phosphate (ACP) phase transition process. The remineralization process and superstructure of the remineralized layer of demineralized dentin were evaluated and analyzed by transmission electron microscope (TEM) and scanning electron microscope (SEM), and the biological stability of the remineralized layer was investigated by collagenase degradation experiment. It demonstrated that Asp promoted the crystallization kinetics of PAA-stabilized amorphous calcium phosphate to hydroxyapatite (HAP), and shortened the remineralization time of demineralized dentin from 7 days to 2 days. The newly formed remineralized dentin had similar morphology and biological stability to the natural dentin layer. The presence of a large number of Asp residues in NCPs promoted the phase transformation of ACP, and further revealed the mechanism of action of NCPs in dentin biomineralization. This experiment also showed that Asp promoted the biomimetic remineralization of dentin; the morphology and hierarchical structure of remineralized layer was similar to that of natural teeth, and had good biological properties.
•Adding aspartic acid notably shortened demineralized dentin remineralization process .•Mineralization effect and biological properties similar to those of natural dentin.•Bone and teeth had similar ultrastructure.•Possible clinical application for carious dentin and resin-dentin bond durability.•Possible clinical application in bone regeneration materials. |
doi_str_mv | 10.1016/j.jmbbm.2020.104226 |
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•Adding aspartic acid notably shortened demineralized dentin remineralization process .•Mineralization effect and biological properties similar to those of natural dentin.•Bone and teeth had similar ultrastructure.•Possible clinical application for carious dentin and resin-dentin bond durability.•Possible clinical application in bone regeneration materials.</description><identifier>ISSN: 1751-6161</identifier><identifier>EISSN: 1878-0180</identifier><identifier>DOI: 10.1016/j.jmbbm.2020.104226</identifier><identifier>PMID: 33302092</identifier><language>eng</language><publisher>Netherlands: Elsevier Ltd</publisher><subject>Amorphous calcium phosphate ; Aspartic Acid ; Biomimetic remineralization ; Calcium Phosphates ; Crystallization ; Dentin ; Dentin sialophosphoprotein ; Kinetics ; Non-collagenous proteins</subject><ispartof>Journal of the mechanical behavior of biomedical materials, 2021-03, Vol.115, p.104226-104226, Article 104226</ispartof><rights>2020</rights><rights>Copyright © 2020. Published by Elsevier Ltd.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c425t-8564788526e3900e86018e75eaf3515fbfae7ae570c8f3001a929c85256840ed3</citedby><cites>FETCH-LOGICAL-c425t-8564788526e3900e86018e75eaf3515fbfae7ae570c8f3001a929c85256840ed3</cites><orcidid>0000-0002-4948-6780 ; 0000-0001-9696-2586</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S1751616120307657$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33302092$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhao, Luyi</creatorcontrib><creatorcontrib>Sun, Jian</creatorcontrib><creatorcontrib>Zhang, Ce</creatorcontrib><creatorcontrib>Chen, Chaoqun</creatorcontrib><creatorcontrib>Chen, Yi</creatorcontrib><creatorcontrib>Zheng, Bo</creatorcontrib><creatorcontrib>Pan, Haihua</creatorcontrib><creatorcontrib>Shao, Changyu</creatorcontrib><creatorcontrib>Jin, Biao</creatorcontrib><creatorcontrib>Tang, Ruikang</creatorcontrib><creatorcontrib>Gu, Xinhua</creatorcontrib><title>Effect of aspartic acid on the crystallization kinetics of ACP and dentin remineralization</title><title>Journal of the mechanical behavior of biomedical materials</title><addtitle>J Mech Behav Biomed Mater</addtitle><description>Type I collagen and non-collagen proteins are the main organic components of dentin. This study aimed to investigate the biomimetic remineralization of demineralized dentin by aspartic acid (Asp), which is abundant in non-collagenous proteins (NCPs). Asp was added to a mineralizing solution containing polyacrylic acid (PAA) to explore the mechanism of Asp regulating the pure amorphous calcium phosphate (ACP) phase transition process. The remineralization process and superstructure of the remineralized layer of demineralized dentin were evaluated and analyzed by transmission electron microscope (TEM) and scanning electron microscope (SEM), and the biological stability of the remineralized layer was investigated by collagenase degradation experiment. It demonstrated that Asp promoted the crystallization kinetics of PAA-stabilized amorphous calcium phosphate to hydroxyapatite (HAP), and shortened the remineralization time of demineralized dentin from 7 days to 2 days. The newly formed remineralized dentin had similar morphology and biological stability to the natural dentin layer. The presence of a large number of Asp residues in NCPs promoted the phase transformation of ACP, and further revealed the mechanism of action of NCPs in dentin biomineralization. This experiment also showed that Asp promoted the biomimetic remineralization of dentin; the morphology and hierarchical structure of remineralized layer was similar to that of natural teeth, and had good biological properties.
•Adding aspartic acid notably shortened demineralized dentin remineralization process .•Mineralization effect and biological properties similar to those of natural dentin.•Bone and teeth had similar ultrastructure.•Possible clinical application for carious dentin and resin-dentin bond durability.•Possible clinical application in bone regeneration materials.</description><subject>Amorphous calcium phosphate</subject><subject>Aspartic Acid</subject><subject>Biomimetic remineralization</subject><subject>Calcium Phosphates</subject><subject>Crystallization</subject><subject>Dentin</subject><subject>Dentin sialophosphoprotein</subject><subject>Kinetics</subject><subject>Non-collagenous proteins</subject><issn>1751-6161</issn><issn>1878-0180</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1PAyEQhonRWL9-gYnh6GXrAAtLDx5M41dioge9eCGUHSJ1PypsTeqvl1rr0ROT4XkZ5iHklMGYAVMX8_G8nc3aMQe-7pScqx1ywHSlC2AadnNdSVYoptiIHKY0B1AAWu-TkRAihyb8gLxee49uoL2nNi1sHIKj1oWa9h0d3pC6uEqDbZrwZYeQe--hw8ykdeBq-kRtV9MauyF0NGKbL6Pdssdkz9sm4cnveURebq6fp3fFw-Pt_fTqoXAll0OhpSorrSVXKCYAqFX-PVYSrReSST_zFiuLsgKnvQBgdsInLvNS6RKwFkfkfPPuIvYfS0yDaUNy2DS2w36ZDC8rAK6VKDMqNqiLfUoRvVnE0Nq4MgzMWqqZmx-pZi3VbKTm1NnvgOWsxfovs7WYgcsNgHnNz4DRJBewc1iHmOWaug__DvgGN52IDw</recordid><startdate>202103</startdate><enddate>202103</enddate><creator>Zhao, Luyi</creator><creator>Sun, Jian</creator><creator>Zhang, Ce</creator><creator>Chen, Chaoqun</creator><creator>Chen, Yi</creator><creator>Zheng, Bo</creator><creator>Pan, Haihua</creator><creator>Shao, Changyu</creator><creator>Jin, Biao</creator><creator>Tang, Ruikang</creator><creator>Gu, Xinhua</creator><general>Elsevier Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-4948-6780</orcidid><orcidid>https://orcid.org/0000-0001-9696-2586</orcidid></search><sort><creationdate>202103</creationdate><title>Effect of aspartic acid on the crystallization kinetics of ACP and dentin remineralization</title><author>Zhao, Luyi ; Sun, Jian ; Zhang, Ce ; Chen, Chaoqun ; Chen, Yi ; Zheng, Bo ; Pan, Haihua ; Shao, Changyu ; Jin, Biao ; Tang, Ruikang ; Gu, Xinhua</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c425t-8564788526e3900e86018e75eaf3515fbfae7ae570c8f3001a929c85256840ed3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Amorphous calcium phosphate</topic><topic>Aspartic Acid</topic><topic>Biomimetic remineralization</topic><topic>Calcium Phosphates</topic><topic>Crystallization</topic><topic>Dentin</topic><topic>Dentin sialophosphoprotein</topic><topic>Kinetics</topic><topic>Non-collagenous proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhao, Luyi</creatorcontrib><creatorcontrib>Sun, Jian</creatorcontrib><creatorcontrib>Zhang, Ce</creatorcontrib><creatorcontrib>Chen, Chaoqun</creatorcontrib><creatorcontrib>Chen, Yi</creatorcontrib><creatorcontrib>Zheng, Bo</creatorcontrib><creatorcontrib>Pan, Haihua</creatorcontrib><creatorcontrib>Shao, Changyu</creatorcontrib><creatorcontrib>Jin, Biao</creatorcontrib><creatorcontrib>Tang, Ruikang</creatorcontrib><creatorcontrib>Gu, Xinhua</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of the mechanical behavior of biomedical materials</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhao, Luyi</au><au>Sun, Jian</au><au>Zhang, Ce</au><au>Chen, Chaoqun</au><au>Chen, Yi</au><au>Zheng, Bo</au><au>Pan, Haihua</au><au>Shao, Changyu</au><au>Jin, Biao</au><au>Tang, Ruikang</au><au>Gu, Xinhua</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effect of aspartic acid on the crystallization kinetics of ACP and dentin remineralization</atitle><jtitle>Journal of the mechanical behavior of biomedical materials</jtitle><addtitle>J Mech Behav Biomed Mater</addtitle><date>2021-03</date><risdate>2021</risdate><volume>115</volume><spage>104226</spage><epage>104226</epage><pages>104226-104226</pages><artnum>104226</artnum><issn>1751-6161</issn><eissn>1878-0180</eissn><abstract>Type I collagen and non-collagen proteins are the main organic components of dentin. This study aimed to investigate the biomimetic remineralization of demineralized dentin by aspartic acid (Asp), which is abundant in non-collagenous proteins (NCPs). Asp was added to a mineralizing solution containing polyacrylic acid (PAA) to explore the mechanism of Asp regulating the pure amorphous calcium phosphate (ACP) phase transition process. The remineralization process and superstructure of the remineralized layer of demineralized dentin were evaluated and analyzed by transmission electron microscope (TEM) and scanning electron microscope (SEM), and the biological stability of the remineralized layer was investigated by collagenase degradation experiment. It demonstrated that Asp promoted the crystallization kinetics of PAA-stabilized amorphous calcium phosphate to hydroxyapatite (HAP), and shortened the remineralization time of demineralized dentin from 7 days to 2 days. The newly formed remineralized dentin had similar morphology and biological stability to the natural dentin layer. The presence of a large number of Asp residues in NCPs promoted the phase transformation of ACP, and further revealed the mechanism of action of NCPs in dentin biomineralization. This experiment also showed that Asp promoted the biomimetic remineralization of dentin; the morphology and hierarchical structure of remineralized layer was similar to that of natural teeth, and had good biological properties.
•Adding aspartic acid notably shortened demineralized dentin remineralization process .•Mineralization effect and biological properties similar to those of natural dentin.•Bone and teeth had similar ultrastructure.•Possible clinical application for carious dentin and resin-dentin bond durability.•Possible clinical application in bone regeneration materials.</abstract><cop>Netherlands</cop><pub>Elsevier Ltd</pub><pmid>33302092</pmid><doi>10.1016/j.jmbbm.2020.104226</doi><tpages>1</tpages><orcidid>https://orcid.org/0000-0002-4948-6780</orcidid><orcidid>https://orcid.org/0000-0001-9696-2586</orcidid></addata></record> |
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subjects | Amorphous calcium phosphate Aspartic Acid Biomimetic remineralization Calcium Phosphates Crystallization Dentin Dentin sialophosphoprotein Kinetics Non-collagenous proteins |
title | Effect of aspartic acid on the crystallization kinetics of ACP and dentin remineralization |
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