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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2021-10-01
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Series: | Scientific Reports |
Online Access: | https://doi.org/10.1038/s41598-021-99186-z |
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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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