Distinct effects of polyphenols and solvents on dentin collagen crosslinking interactions and biostability.
Distinct effects of polyphenols and solvents on dentin collagen crosslinking interactions and biostability.
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DOI：
10.1016/j.dental.2021.09.009
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发表时间：
2021-12
期刊：
影响因子：
--
通讯作者：
Wang Y
中科院分区：
文献类型：
--
作者：
Hass V;Liu H;Cook W;Walker MP;Wang Y
目的：评价不同多酚类物质和不同溶剂对牙本质胶原蛋白的交联作用及其对基质金属蛋白酶和胶原酶降解的生物稳定性的影响。以乙醇(EtOH)和二甲基亚砜(DMSO)为溶剂，制备了两种不同水溶性的多酚[原花青素(PA)和槲皮素(QC)]。从第三磨牙牙本质板上切下6微米厚的牙本质膜。脱矿后，薄膜或板材经过60-S处理(PA或QC)或不处理(对照)，然后用原始溶剂(Etoh或DMSO)或蒸馏水(DW)进行延伸漂洗。用傅立叶变换红外光谱检测胶原蛋白的相互作用。通过激光共聚焦扫描显微镜检测内源性MMPs活性，以及通过失重、羟脯氨酸释放和扫描电子显微镜检测外源性胶原酶降解来评价其生物稳定性。最后，还对胶原酶的直接灭活进行了评价。数据分析采用三因素方差分析和组后检验(α=0.05%)。观察到两种多酚和不同溶剂对胶原蛋白的交联和生物稳定性的影响。与QC相比，PA具有更高的交联度和生物稳定性(p<；0.001)，显示出可以忽略的胶原蛋白相互作用。使用DMSO溶剂时，两种多酚的药效结果都显著降低(p<；0.05)。DMSO漂洗进一步削弱了PA与胶原的相互作用，降低了生物稳定性(p<；0.05)。QC和DW-Rresse检测到生物稳定性较低，这表明由于胶原蛋白的物理存在而直接受到酶的抑制。胶原蛋白的相互作用和生物稳定性取决于多酚的化学特性。处理-溶液溶剂可能会影响多酚与胶原之间的相互作用，特别是DMSO对胶原的交联性和生物稳定性显示出不利的影响，应谨慎使用。
To evaluate the effects of different polyphenols and solvents on dentin collagen’s crosslinking interactions and biostabilization against MMPs and collagenase degradation. Two polyphenols [proanthocyanidin (PA) and quercetin (QC)] with different water solubility were prepared as treatment solutions using ethanol (EtOH) or dimethyl sulfoxide (DMSO) as solvents. 6-um-thick dentin films were microtomed from dentin slabs of third molars. Following demineralization, films or slabs were subject to 60-s treatment (PA or QC) or no treatment (control) with subsequent extended-rinse with original solvent (EtOH or DMSO) or distilled water (DW). Collagen crosslinking interactions were assessed by FTIR. Biostability was assessed through endogenous MMPs activity via confocal laser scanning microscopy, and exogenous collagenase degradation via weight loss, hydroxyproline release and SEM. Finally, direct collagenase inactivation was also evaluated. Data were analyzed by three-way ANOVA and post-hoc tests (α=0.05%). Distinct effects of two polyphenols and solvents on collagen crosslinking and biostabilization were observed. Higher crosslinking and biostability efficacy occurred with PA than QC (p < 0.001) that demonstrated negligible collagen interactions. With DMSO solvent, efficacy results were significantly reduced with both polyphenols (p < 0.05). DMSO-rinse further weakened interactions of PA with collagen, diminishing biostability (p < 0.05). Low biostability was detected with QC and DW-rinse, suggesting direct enzymatic inhibition due to physical presence in collagen. Collagen crosslinking interactions and biostability depend on polyphenol chemical characteristics. Treatment-solution solvents may affect interactions between polyphenols and collagen, specifically, DMSO showed detrimental effects on collagen crosslinking and biostability and should be used with caution.
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