Theaflavins as a novel cross-linker quickly stabilize demineralized dentin collagen against degradation.
Theaflavins as a novel cross-linker quickly stabilize demineralized dentin collagen against degradation.
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DOI：
10.1038/s41598-021-99186-z
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发表时间：
2021-10-05
影响因子：
4.6
通讯作者：
Wang Y
中科院分区：
文献类型：
--
作者：
Liu H;Guo J;Wang R;Wang Y
目的：探讨红茶中的茶黄素(Tf)在临床相关条件下，通过交联剂的作用对牙本质胶原蛋白的保护作用。从人磨牙牙本质板上切下10微米厚的牙本质膜。脱矿后，用两种浓度(0.4%和2%)的TF处理薄膜或平板30分钟，S(音译)，并以著名的胶原交联剂葡萄籽原花青素(PA)为对照。用傅里叶变换红外光谱、失重、羟脯氨酸释放和扫描/透射电子显微镜研究了胶原蛋白的交联相互作用和抗酶降解稳定性。资料分析采用单因素方差分析、图基检验和学生t检验(α = 为0.05%)。结果表明，胶原蛋白的交联和稳定效果依赖于TF/PA的浓度。在2.0%时，TF和PA对胶原几乎完全保护；在0.4%时，TF对胶原的稳定效果明显好于PA(P <； 0.05)，而未经处理的胶原被完全消化。结论是，TF在临床相关时间内(S 30分钟)使牙本质胶原交联化，对胶原蛋白的酶降解具有极好的保护作用，疗效与PA相当或更好。这项研究支持了TF作为一种新型的、有前途的胶原交联剂在复合修复体中用于抗降解、持久的牙本质粘结的潜在用途。
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.