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Mussel-inspired polymer with catechol and cationic Lys functionalities for dentin wet bonding
Mussels can form tough and long-lasting adhesions to organic and inorganic surfaces in saline and impactive severe aquatic environments. Similar to mussel adhesion, dentin bonding occurs in a wet environment. However, unlike mussels, it is difficult to achieve long-lasting bonds with dentin. Moreove...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9719097/ https://www.ncbi.nlm.nih.gov/pubmed/36471892 http://dx.doi.org/10.1016/j.mtbio.2022.100506 |
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author | Hu, Zunhan Wu, Wenzhen Yu, Meizhe Wang, Zhi Yang, Zhenyu Xing, Xiaodong Chen, Xiaofang Niu, Lina Yu, Fan Xiao, Yuhong Chen, Jihua |
author_facet | Hu, Zunhan Wu, Wenzhen Yu, Meizhe Wang, Zhi Yang, Zhenyu Xing, Xiaodong Chen, Xiaofang Niu, Lina Yu, Fan Xiao, Yuhong Chen, Jihua |
author_sort | Hu, Zunhan |
collection | PubMed |
description | Mussels can form tough and long-lasting adhesions to organic and inorganic surfaces in saline and impactive severe aquatic environments. Similar to mussel adhesion, dentin bonding occurs in a wet environment. However, unlike mussels, it is difficult to achieve long-lasting bonds with dentin. Moreover, water is considered a major hindrance in dentin bonding. Inspired by the synergistic effect of cationic lysine (Lys) and catechol on the elimination of the hydration layer during mussel adhesion, a catechol- and Lys-functionalized polymerizable polymer (catechol–Lys–methacrylate [CLM]) was synthesized to replicate the complex synergy between amino acids and catechol. The bond-promoting potential of 5 mg/mL CLM primer was confirmed using an in vitro wet dentin-bonding model, which was characterized by an improvement in bond strength and durability. CLM can adhere to wet demineralized dentin, with Lys acting as a molecular vanguard to expel water. Subsequently, a myriad of interfacial interactions can be obtained by introducing the catechol group into the interface. Additionally, tough and long-lasting adhesion, similar to that formed by mussels, can be achieved by grafting CLM onto type I collagen via covalent bonds, hydrogen bonds, Van der Waals interactions, and cation–π interactions, which can enhance the mechanical and chemical stability of collagen, increase the enzymatic resistance of collagen, and provide additional physical/chemical adhesion to dentin bonds. Catechol- and cationic Lys-functionalized polymers can improve the stability of the resin–dentin interface under wet conditions. |
format | Online Article Text |
id | pubmed-9719097 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-97190972022-12-04 Mussel-inspired polymer with catechol and cationic Lys functionalities for dentin wet bonding Hu, Zunhan Wu, Wenzhen Yu, Meizhe Wang, Zhi Yang, Zhenyu Xing, Xiaodong Chen, Xiaofang Niu, Lina Yu, Fan Xiao, Yuhong Chen, Jihua Mater Today Bio Full Length Article Mussels can form tough and long-lasting adhesions to organic and inorganic surfaces in saline and impactive severe aquatic environments. Similar to mussel adhesion, dentin bonding occurs in a wet environment. However, unlike mussels, it is difficult to achieve long-lasting bonds with dentin. Moreover, water is considered a major hindrance in dentin bonding. Inspired by the synergistic effect of cationic lysine (Lys) and catechol on the elimination of the hydration layer during mussel adhesion, a catechol- and Lys-functionalized polymerizable polymer (catechol–Lys–methacrylate [CLM]) was synthesized to replicate the complex synergy between amino acids and catechol. The bond-promoting potential of 5 mg/mL CLM primer was confirmed using an in vitro wet dentin-bonding model, which was characterized by an improvement in bond strength and durability. CLM can adhere to wet demineralized dentin, with Lys acting as a molecular vanguard to expel water. Subsequently, a myriad of interfacial interactions can be obtained by introducing the catechol group into the interface. Additionally, tough and long-lasting adhesion, similar to that formed by mussels, can be achieved by grafting CLM onto type I collagen via covalent bonds, hydrogen bonds, Van der Waals interactions, and cation–π interactions, which can enhance the mechanical and chemical stability of collagen, increase the enzymatic resistance of collagen, and provide additional physical/chemical adhesion to dentin bonds. Catechol- and cationic Lys-functionalized polymers can improve the stability of the resin–dentin interface under wet conditions. Elsevier 2022-11-26 /pmc/articles/PMC9719097/ /pubmed/36471892 http://dx.doi.org/10.1016/j.mtbio.2022.100506 Text en © 2022 The Authors https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Full Length Article Hu, Zunhan Wu, Wenzhen Yu, Meizhe Wang, Zhi Yang, Zhenyu Xing, Xiaodong Chen, Xiaofang Niu, Lina Yu, Fan Xiao, Yuhong Chen, Jihua Mussel-inspired polymer with catechol and cationic Lys functionalities for dentin wet bonding |
title | Mussel-inspired polymer with catechol and cationic Lys functionalities for dentin wet bonding |
title_full | Mussel-inspired polymer with catechol and cationic Lys functionalities for dentin wet bonding |
title_fullStr | Mussel-inspired polymer with catechol and cationic Lys functionalities for dentin wet bonding |
title_full_unstemmed | Mussel-inspired polymer with catechol and cationic Lys functionalities for dentin wet bonding |
title_short | Mussel-inspired polymer with catechol and cationic Lys functionalities for dentin wet bonding |
title_sort | mussel-inspired polymer with catechol and cationic lys functionalities for dentin wet bonding |
topic | Full Length Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9719097/ https://www.ncbi.nlm.nih.gov/pubmed/36471892 http://dx.doi.org/10.1016/j.mtbio.2022.100506 |
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