Abstract
The formation of a hybrid layer is essential for successful dentin bonding and is achieved by adhesive penetration between exposed collagen fibrils in the demineralized dentin. Incomplete infiltration of the adhesive within the collagen network results in exposed fibrils, which may suffer enzymatic degradation over time. Methods to increase collagen resistance to proteinases (enzymes that degrade proteins) have been studied. One particular approach is to use collagen cross‐linking agents that modify collagen through addition of specific or random amino acid linkage between and within its molecules. This Critical Appraisal provides information on the effects of various cross‐linkers on dentin collagen stability, dentin properties, and resin–dentin bond strengths, and calls for critical thinking on the potential effects of this therapeutic approach.
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