Dentin Bonding: Matrix Metalloproteinases and Chlorhexidine

Abstract

Contemporary resin–dentin bonding is initiated by systems that use phosphoric acid or acidic resin monomers to remove mineral, exposing the superficial dentin collagen matrix. Collagen-associated proteins, including enzymes known as matrix metalloproteinases (MMPs), also are exposed. The collagen matrix is subsequently infiltrated with resins that are polymerized to establish an adhesive attachment to the dentin. Exposed collagen matrix that is not infiltrated with the adhesive can be degraded by associated MMPs, which might result in deterioration of the adhesive–dentin bond over time. Chlorhexidine (CHX) is able to inhibit MMPs by binding calcium and zinc ions necessary for proteolytic activity. This Critical Appraisal presents salient publications on research that evaluate CHX and its ability to limit MMP degradation of dentin bonds created by etch-and-rinse and self-etch adhesive systems.