The effect of kaempferol on the dentin bonding stability through matrix metalloproteinases inhibition and collagen crosslink in dentin biomodification

牙本质 化学 基质金属蛋白酶 胶粘剂 傅里叶变换红外光谱 粘结强度 酶谱 核化学 复合材料 化学工程 材料科学 生物化学 有机化学 图层(电子) 工程类
作者
Jeonghwa Cho,Hyeryeong Kim,Kyung-Hyeon Yoo,Youna Paik,In‐Ryoung Kim,Seog-Young Yoon,Yong‐Il Kim
出处
期刊:Journal of Dental Sciences [Elsevier]
卷期号:18 (3): 1023-1030 被引量:4
标识
DOI:10.1016/j.jds.2022.12.002
摘要

Naturally derived collagen crosslinkers with matrix metalloproteinases (MMPs) inhibitory activity for dentin bonding have been previously studied. One of these crosslinkers is flavonoids. The purpose of this study was to investigate whether dentin pretreatment with kaempferol (KEM), one of the flavonoids, enhances dentin bond stability and nanoleakage at the dentin-resin interface through MMPs inhibition and collagen crosslinking. The experimental KEM-containing solution was used to pretreat demineralized dentin prior to the application of a universal adhesive. KEM is a natural flavonoid and those which did not take the experimental solution served as the control group (CON). Microtensile bond strength (μTBS) and nanoleakage tests were conducted before and after the thermocycling to evaluate the influence of KEM on dentin bond strength. The MMPs inhibition activity of KEM was analyzed via MMPs zymography using a confocal microscopy. Fourier-transform infrared (FTIR) spectroscopy was used to demonstrate that KEM inhibits MMPs and enhances collagen crosslinking. The μTBS values of KEM group exhibited a higher bond strength after thermocycling. At the resin-dentin interface, the KEM group did not exhibit any signs of nanoleakage after thermocycling. Furthermore, MMPs zymography confirmed that there was a relatively low activity of MMPs in the presence of KEM. In FTIR analysis, the PO4 peak representing the cross-link between dentin and collagen was significantly higher in the KEM group. Our findings suggest that pretreatment with KEM enhances the dentin bonding stability at the resin-dentin interface by acting as a collagen crosslinker and MMPs inhibitor.

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