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Objectives
Collagen fibrils from carious dentin matrix are prone to enzymatic degradation. This study investigates the feasibility and mechanism of nordihydroguaiaretic acid (NDGA), as a collagen crosslinker, to bio‐modify the demineralized dentin matrix.
Methods
The physicochemical properties of the crosslinked dentin matrix were characterized by swelling ratio, ninhydrin assay, Fourier Transform...
Enzymatic degradation of demineralized collagen matrix seriously impairs durable resin-dentin bonding. In this study, we evaluated the effect of nordihydroguaiaretic acid (NDGA)-modified etchant on the resistance to enzymatic degradation and mechanical properties of demineralized collagen matrix. Dentin beams were randomly demineralized by following solutions: 1) 10% phosphoric acid (PhA) solution,...
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