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Effect of polyhydroxy-terminated PAMAM dendrimer on dentin matrix metalloproteinases within the hybrid layers

BACKGROUND: Intrafibrillar remineralization within the hybrid layers (HLs) has recently attracted extensive attention in achieving durable resin-dentin bonds. The polyhydroxy-terminated poly(amidoamine) dendrimer (PAMAM-OH) at fourth generation becomes a desirable candidate to induce intrafibrillar...

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Autores principales: Luo, Yu, Si, Ruirui, He, Yuan, Wang, Mengmeng, Yu, Yingying, Huang, Xin, Huang, Rong, Huang, Yingyi, Luo, Yang, Jin, Wei, Gou, Yaping
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10007817/
https://www.ncbi.nlm.nih.gov/pubmed/36906526
http://dx.doi.org/10.1186/s12903-023-02841-2
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author Luo, Yu
Si, Ruirui
He, Yuan
Wang, Mengmeng
Yu, Yingying
Huang, Xin
Huang, Rong
Huang, Yingyi
Luo, Yang
Jin, Wei
Gou, Yaping
author_facet Luo, Yu
Si, Ruirui
He, Yuan
Wang, Mengmeng
Yu, Yingying
Huang, Xin
Huang, Rong
Huang, Yingyi
Luo, Yang
Jin, Wei
Gou, Yaping
author_sort Luo, Yu
collection PubMed
description BACKGROUND: Intrafibrillar remineralization within the hybrid layers (HLs) has recently attracted extensive attention in achieving durable resin-dentin bonds. The polyhydroxy-terminated poly(amidoamine) dendrimer (PAMAM-OH) at fourth generation becomes a desirable candidate to induce intrafibrillar remineralization to protect exposed collagen fibrils within HLs based on the size exclusion effect of fibrillar collagen. However, the remineralization process in vivo is time-consuming, during which the exposed collagen fibrils are vulnerable to enzymatic degradation, resulting in unsatisfactory remineralization. Thereby, if PAMAM-OH itself possesses concomitant anti-proteolytic activity during the induction of remineralization, it would be very beneficial to obtain satisfactory remineralization. METHODS: Binding capacity tests using adsorption isotherm and confocal laser scanning microscopy (CLSM) were performed to assess if the PAMAM-OH had adsorption capacity on dentin. Anti-proteolytic testings were detected by MMPs assay kit, in-situ zymography and ICTP assay. Adhesive infiltration of resin-dentin interface and tensile bond strength before and after thermomechanical cycling were implemented to assess if the PAMAM-OH adversely affected resin-dentin bonds. RESULTS: Anti-proteolytic testings performed using MMPs assay kit, in-situ zymography and ICTP assay indicated that PAMAM-OH inhibited exogenous soluble MMP-9 as well as had inhibitory effect on the endogenous proteases. Adhesive infiltration of resin-dentin interface and tensile bond strength before and after thermomechanical cycling were implemented to indicate that the PAMAM-OH pretreatment had no adverse effects on immediate dentin bonding and prolonged the durability of resin-dentin bonds. CONCLUSIONS: PAMAM-OH possesses anti-proteolytic activity and prevents exposed collagen fibrils within HLs from degradation, which lays the foundation for the satisfactory intrafibrillar remineralization induced by PAMAM-OH within HLs to achieve durable resin-dentin bonds in the next work.
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spelling pubmed-100078172023-03-12 Effect of polyhydroxy-terminated PAMAM dendrimer on dentin matrix metalloproteinases within the hybrid layers Luo, Yu Si, Ruirui He, Yuan Wang, Mengmeng Yu, Yingying Huang, Xin Huang, Rong Huang, Yingyi Luo, Yang Jin, Wei Gou, Yaping BMC Oral Health Research BACKGROUND: Intrafibrillar remineralization within the hybrid layers (HLs) has recently attracted extensive attention in achieving durable resin-dentin bonds. The polyhydroxy-terminated poly(amidoamine) dendrimer (PAMAM-OH) at fourth generation becomes a desirable candidate to induce intrafibrillar remineralization to protect exposed collagen fibrils within HLs based on the size exclusion effect of fibrillar collagen. However, the remineralization process in vivo is time-consuming, during which the exposed collagen fibrils are vulnerable to enzymatic degradation, resulting in unsatisfactory remineralization. Thereby, if PAMAM-OH itself possesses concomitant anti-proteolytic activity during the induction of remineralization, it would be very beneficial to obtain satisfactory remineralization. METHODS: Binding capacity tests using adsorption isotherm and confocal laser scanning microscopy (CLSM) were performed to assess if the PAMAM-OH had adsorption capacity on dentin. Anti-proteolytic testings were detected by MMPs assay kit, in-situ zymography and ICTP assay. Adhesive infiltration of resin-dentin interface and tensile bond strength before and after thermomechanical cycling were implemented to assess if the PAMAM-OH adversely affected resin-dentin bonds. RESULTS: Anti-proteolytic testings performed using MMPs assay kit, in-situ zymography and ICTP assay indicated that PAMAM-OH inhibited exogenous soluble MMP-9 as well as had inhibitory effect on the endogenous proteases. Adhesive infiltration of resin-dentin interface and tensile bond strength before and after thermomechanical cycling were implemented to indicate that the PAMAM-OH pretreatment had no adverse effects on immediate dentin bonding and prolonged the durability of resin-dentin bonds. CONCLUSIONS: PAMAM-OH possesses anti-proteolytic activity and prevents exposed collagen fibrils within HLs from degradation, which lays the foundation for the satisfactory intrafibrillar remineralization induced by PAMAM-OH within HLs to achieve durable resin-dentin bonds in the next work. BioMed Central 2023-03-11 /pmc/articles/PMC10007817/ /pubmed/36906526 http://dx.doi.org/10.1186/s12903-023-02841-2 Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/ (https://creativecommons.org/publicdomain/zero/1.0/) ) applies to the data made available in this article, unless otherwise stated in a credit line to the data.
spellingShingle Research
Luo, Yu
Si, Ruirui
He, Yuan
Wang, Mengmeng
Yu, Yingying
Huang, Xin
Huang, Rong
Huang, Yingyi
Luo, Yang
Jin, Wei
Gou, Yaping
Effect of polyhydroxy-terminated PAMAM dendrimer on dentin matrix metalloproteinases within the hybrid layers
title Effect of polyhydroxy-terminated PAMAM dendrimer on dentin matrix metalloproteinases within the hybrid layers
title_full Effect of polyhydroxy-terminated PAMAM dendrimer on dentin matrix metalloproteinases within the hybrid layers
title_fullStr Effect of polyhydroxy-terminated PAMAM dendrimer on dentin matrix metalloproteinases within the hybrid layers
title_full_unstemmed Effect of polyhydroxy-terminated PAMAM dendrimer on dentin matrix metalloproteinases within the hybrid layers
title_short Effect of polyhydroxy-terminated PAMAM dendrimer on dentin matrix metalloproteinases within the hybrid layers
title_sort effect of polyhydroxy-terminated pamam dendrimer on dentin matrix metalloproteinases within the hybrid layers
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10007817/
https://www.ncbi.nlm.nih.gov/pubmed/36906526
http://dx.doi.org/10.1186/s12903-023-02841-2
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