Dentin collagen and collagenolytic enzymes

Dentin collagen and collagenolytic enzymes represent a critical therapeutic target system in restorative dentistry, primarily focused on the preservation of the resin-dentin bond and the management of dental caries [1, 2]. The dentin organic matrix is composed of approximately 90% Type I collagen, which provides the structural scaffold for mineralization [2, 3]. Within this matrix, endogenous enzymes such as matrix metalloproteinases (MMPs) and cysteine cathepsins are sequestered in inactive pro-forms during tooth development [4, 5]. These enzymes can be activated by acidic environments, such as those created by bacterial acids in caries or by acidic etchants and monomers used in dental bonding procedures [2, 4]. Once active, they catalyze the hydrolytic degradation of exposed collagen fibrils, leading to the failure of the hybrid layer in composite restorations and the progression of dental decay [1, 5]. Therapeutic strategies target this system through the use of protease inhibitors like chlorhexidine or cross-linking agents like carbodiimides, which either silence the enzymes or reinforce the collagen matrix against proteolysis [1, 3]. This target system is unique because it involves both host-derived enzymes and the structural integrity of the tooth substrate itself. Effective modulation of this complex is essential for improving the longevity of modern adhesive dental treatments.

Other names

Dentin organic matrixEndogenous dentin proteasesDentin-bound MMPs and cathepsinsHybrid layer proteases

Inhibition of endogenous protease activity (MMPs and cysteine cathepsins) and stabilization of the collagen matrix through cross-linking to prevent hydrolytic degradation [1, 3, 5].