Einfluss der Verhinderung der Kollagen-Degradation durch MMPs auf den Dentin-Klebeverbund

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Type I collagen plays an important role in the determination of resin-dentin bonding durability. Recently, our results and in vitro and in vivo studies demonstrated that the hydrolytic degradation of dentin collagen fibrils in and under resin-dentin bonding interfaces significantly decreases the bonding durability. It is well accepted that the degradation of the dentinal collagen matrix is caused by Matrix Metalloproteinases (MMPs) - a family of zinc-dependent host-derived proteolytic enzymes, which are present in dentinal and can be activated by modern self-etch and etch-and-rinse adhesives. Inhibition of MMPs by a suitable complexing agent for zinc may slow down or prevent the degradation of dentinal collagen. And it is very urgent to incorporate MMP-inhibitory functionality into dentin adhesives to inhibite the activation of MMPs during bonding procedure. Therefore, in a multidisciplinary approach, we propose that a novel bio-functional macromonomer, as a biocompatible component in adhesives, possesses durable MMPs-inhibitory property and can inhibit collagen degradation in resin bonding to dentin. And it may promote the remineralization of decalcified dentin, allowing for natural healing of caries lesions. This new concept will significantly contribute to improving durability of resin-dentin bonds. At a lager scale, the macromonomer with MMPs-inhibitory property may be further applied to implantology and periodontology to inhibit pathological tissue destruction caused by collagen degradation.