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Dentin is a calcified tissue of the tooth, consisting of an inorganic mineral phase and an organic matrix. The organic matrix is predominantly composed of Type I collagen (approx. 90%), which provides a scaffold for mineralization, and non-collagenous proteins (NCPs) such as dentin sialophosphoprotein (DSPP) and dentin matrix protein 1 (DMP1) that regulate hydroxyapatite formation [1, 3]. Dentinal tubules traverse the dentin, containing odontoblastic processes and fluid; proteins within these tubules and the surrounding matrix are critical for tooth sensitivity and regenerative responses [4]. In clinical practice, these proteins are targets for desensitizing agents that occlude tubules and for protease inhibitors like chlorhexidine that prevent the degradation of collagen by matrix metalloproteinases (MMPs) during dental bonding [2]. Understanding the interaction between dental materials and the dentin organic matrix is essential for improving the longevity of restorative treatments and managing conditions like dentinogenesis imperfecta [3].
Occlusion of dentinal tubules to reduce hydrodynamic fluid movement, inhibition of endogenous matrix metalloproteinases (MMPs) to prevent collagen network degradation, and cross-linking of collagen fibrils to enhance mechanical stability.
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