Theaflavins as a novel cross-linker quickly stabilize demineralized dentin collagen against degradation

Abstract To investigate the ability of theaflavins (TF) from black tea to protect dentin collagen against enzymatic degradation via cross-linking effect under clinically relevant conditions. 10-µm-thick dentin films were microtomed from dentin slabs of human molars. Following demineralization, films...

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Main Authors: Hang Liu, Jing Guo, Rong Wang, Yong Wang
Format: Article
Language:English
Published: Nature Publishing Group 2021-10-01
Series:Scientific Reports
Online Access:https://doi.org/10.1038/s41598-021-99186-z
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spelling doaj-c2e78a0e037c4d8cb76b78cf49e53fa92021-10-10T11:27:19ZengNature Publishing GroupScientific Reports2045-23222021-10-0111111110.1038/s41598-021-99186-zTheaflavins as a novel cross-linker quickly stabilize demineralized dentin collagen against degradationHang Liu0Jing Guo1Rong Wang2Yong Wang3School of Dentistry, University of Missouri – Kansas CitySchool of Dentistry, University of Missouri – Kansas CitySchool of Dentistry, University of Missouri – Kansas CitySchool of Dentistry, University of Missouri – Kansas CityAbstract To investigate the ability of theaflavins (TF) from black tea to protect dentin collagen against enzymatic degradation via cross-linking effect under clinically relevant conditions. 10-µm-thick dentin films were microtomed from dentin slabs of human molars. Following demineralization, films or slabs were treated with TF at two concentrations (0.4% and 2%) for 30 s. A well-known collagen cross-linker grape seed proanthocyanidins (PA) was used as control. Collagen cross-linking interactions and stabilization against enzymatic degradation were investigated by Fourier transform infrared spectroscopy, weight loss, hydroxyproline release, and scanning/transmission electron microscopy. Data were analyzed by ANOVA, Tukey’s and Student’s T test (α = 0.05%). The results showed collagen cross-linking and stabilization efficacy was dependent on TF/PA concentrations. At 2.0%, TF and PA offered nearly full protection to collagen; at 0.4%, TF exhibited a significantly better collagen stabilization effect than PA (P < 0.05), while untreated collagen was completely digested. It’s concluded that TF cross-links dentin collagen within a clinically relevant time (30 s) and offers excellent collagen protection against enzymatic degradation, with efficacy comparable to or better than PA. The study supports the potential use of TF as a novel, promising collagen cross-linker for degradation resistant, long-lasting dentin bonding in composite restorations.https://doi.org/10.1038/s41598-021-99186-z
collection DOAJ
language English
format Article
sources DOAJ
author Hang Liu
Jing Guo
Rong Wang
Yong Wang
spellingShingle Hang Liu
Jing Guo
Rong Wang
Yong Wang
Theaflavins as a novel cross-linker quickly stabilize demineralized dentin collagen against degradation
Scientific Reports
author_facet Hang Liu
Jing Guo
Rong Wang
Yong Wang
author_sort Hang Liu
title Theaflavins as a novel cross-linker quickly stabilize demineralized dentin collagen against degradation
title_short Theaflavins as a novel cross-linker quickly stabilize demineralized dentin collagen against degradation
title_full Theaflavins as a novel cross-linker quickly stabilize demineralized dentin collagen against degradation
title_fullStr Theaflavins as a novel cross-linker quickly stabilize demineralized dentin collagen against degradation
title_full_unstemmed Theaflavins as a novel cross-linker quickly stabilize demineralized dentin collagen against degradation
title_sort theaflavins as a novel cross-linker quickly stabilize demineralized dentin collagen against degradation
publisher Nature Publishing Group
series Scientific Reports
issn 2045-2322
publishDate 2021-10-01
description Abstract To investigate the ability of theaflavins (TF) from black tea to protect dentin collagen against enzymatic degradation via cross-linking effect under clinically relevant conditions. 10-µm-thick dentin films were microtomed from dentin slabs of human molars. Following demineralization, films or slabs were treated with TF at two concentrations (0.4% and 2%) for 30 s. A well-known collagen cross-linker grape seed proanthocyanidins (PA) was used as control. Collagen cross-linking interactions and stabilization against enzymatic degradation were investigated by Fourier transform infrared spectroscopy, weight loss, hydroxyproline release, and scanning/transmission electron microscopy. Data were analyzed by ANOVA, Tukey’s and Student’s T test (α = 0.05%). The results showed collagen cross-linking and stabilization efficacy was dependent on TF/PA concentrations. At 2.0%, TF and PA offered nearly full protection to collagen; at 0.4%, TF exhibited a significantly better collagen stabilization effect than PA (P < 0.05), while untreated collagen was completely digested. It’s concluded that TF cross-links dentin collagen within a clinically relevant time (30 s) and offers excellent collagen protection against enzymatic degradation, with efficacy comparable to or better than PA. The study supports the potential use of TF as a novel, promising collagen cross-linker for degradation resistant, long-lasting dentin bonding in composite restorations.
url https://doi.org/10.1038/s41598-021-99186-z
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