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Published on: July 10, 2014
Anti-proteolytic property and bonding durability of mussel adhesive protein-modified dentin adhesive interface
Hui Fang1, Quan-Li Li1, Min Han1
1College & Hospital of Stomatology, Key Lab of Oral Diseases Research of Anhui Province, Anhui Medical University, Hefei 230032, China.
Objectives:
To evaluate the effect of mussel adhesive protein (MAP) on collagenase activity, dentin collagen degradation and microtensile dentin bond strength (μTBS).
Methods:
Three groups were designed: 1. experimental group: treated with MAP; 2. positive control: treated with GM6001 (collagenase-inhibitor); 3. negative control: treated with distilled water (DW). For collagenase activity, Clostridiopeptidase-A was added to each group (n=5), and collagenase activity was assessed by colorimetric assay. For dentin collagen degradation, thirty dentin slabs were allocated to the three above groups (n=10). Dentin collagen degradation was evaluated by measuring released hydroxyproline by colorimetric assay after being incubated in Clostridiopeptidase-A for 7 days. For microtensile bond strength, sixty human third molars with flat dentin surfaces were etched by phosphoric acid and then assigned to the three above groups (n=20). An etch-and-rinse adhesive system was applied to all three groups as stated in standard clinic protocol. The test of μTBS was performed before and after thermocycling and collagenase challenge.
Results:
The collagenase activities (nmol/min/mg) in the group of MAP was significantly less inactive compared to the group of GM6001 and DW (MAP
Significance:
MAP inhibits collagenase activity, prevents dentin collagen degradation, and delays the deterioration of the dentin bonding of composite restoration over time.
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