La clorhexidina como inhibidor de las metaloproteinasas en la dentina: implicaciones para la estabilidad de la interfaz adhesiva.
DOI:
https://doi.org/10.36557/2674-8169.2026v8n7p408-434Keywords:
Chlorhexidine, Matrix metalloproteinases, Dentin, Hybrid layer, Dentin bondingAbstract
The stability of the dentin adhesive interface remains one of the main challenges in contemporary restorative dentistry, especially due to the progressive degradation of the hybrid layer and exposed collagen matrix. In this context, matrix metalloproteinases (MMPs), endogenous enzymes present in dentin, play an important role in collagen degradation and in the reduction of bond strength over time. Chlorhexidine has been investigated as an inhibitor of these enzymes, showing potential to preserve the organic matrix and improve the longevity of resin-dentin bonding. This study aimed to analyze the role of chlorhexidine as a matrix metalloproteinase inhibitor in dentin and its implications for the stability of the adhesive interface. This is an integrative literature review conducted in PubMed/MEDLINE, SciELO, ScienceDirect/Elsevier and Connected Papers databases, including in vitro and in vivo studies, clinical trials, systematic reviews, meta-analyses and classic studies related to dentin bonding, hybrid layer, MMPs and chlorhexidine. The findings indicate that chlorhexidine may reduce the proteolytic activity of MMPs through interaction with metal ions essential for their catalytic function, contributing to the preservation of the hybrid layer, mainly in etch-and-rinse systems. However, its effectiveness is variable and depends on the adhesive system, concentration, application time and clinical protocol. It is concluded that chlorhexidine plays a relevant role in preserving the adhesive interface, although it cannot independently prevent all degradation mechanisms.
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Copyright (c) 2026 Ana Clara Cândido Vasconcelos, Thallison Matheus Lisboa Fernandes , Michelle Leão Bittencourt Brandão Medeiros
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