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.

Highlights

  • 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

  • We reported that PA was capable of cross-linking demineralized dentin (DD) layer within a clinically relevant time of 15–30 ­s21,22, which is very important since longer treatment time is generally not feasible in clinical settings where patients are treated with mouth open and the procedure time

  • It is very difficult to find out a clear relationship between specific chemical structure and the crosslinking property from the studies of PA because of the difficulty in separating each compound from PA, especially the high molecular weight (MW) species, which are believed to be more effective than lower MW species in collagen ­interactions[24]

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Summary

Introduction

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. 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. Enzymatic degradation of unprotected demineralized collagen by MMPs as well as other host-derived enzymes (such as cysteine cathepsins) causes interface breakdown, eventually leading to the failure of the composite ­restoration[9,10] To solve this degradation issue, collagen cross-linkers have been applied to the interface and their protection efficacies have been s­ tudied[11,12]. The degradation resistance of dentin collagen could be improved by EGCG or EGC, their effects were not as good as PA (less than 50% protection)[24] Besides monomeric catechins, another type of polyphenols, theaflavins (TF), is abundant in tea extracts, especially from black tea (Camellia sinensis). The null hypotheses tested were that TF would not be able to (1) crosslink dentin collagen via chemical interactions or (2) stabilize dentin collagen against enzymatic degradation

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