貽貝粘附蛋白改性的樹脂—牙本質(zhì)粘接界面的抗蛋白水解性及粘接耐久性的研究
[Abstract]:Objective A layer of exposed collagen fibers always exists at the bottom of the mixed layer in the contemporary dentin bonding system, whether it is etch-rinse adhesive or self-etch adhesive. The purpose of this study was to investigate the effects of mussel adhesion protein on the activity of collagenase, the degradation of dentin collagen and the micro-tensile strength of dentin adhesion, so as to improve the durability of dentin adhesion. Inhibition of collagenase activity was detected by kit test. 1 mg/ml Mussel Adhesion Protein and 100U/ml type VII collagenase (one of the representative types of matrix metalloproteinase) were used as experimental group; GM6001 (a known synthetic inhibitor of matrix metalloproteinase) and 100U/ml type VII collagenase were used as positive control group; distilled water and 100U/ml type VII collagenase were used as distilled water and 100U/ml type VII collagenase were used as positive control group. Each group was divided into five subgroups (n=5). After full reaction, the basal fluid was added and the inhibition degree of enzyme activity was measured by spectrophotometry at 412 nm. To evaluate the inhibitory effect of mussel adhesion protein on dentin collagenase hydrolysis, 30 pieces of human dentin tablets were randomly divided into three groups (n=10): mussel adhesion protein group, GM6001 group, distillation. After demineralization, the dentin tablets were incubated in collagenase solution for 7 days. The content of hydroxyproline in the supernatant was measured to evaluate the degree of collagen degradation. According to the different pretreatment methods after etching and rinsing, they were randomly divided into three groups: mussel adhesive protein group, GM6001 group and distilled water group.The bonded specimens were prepared into resin-dentin bonding strips, and then divided into two subgroups according to whether the bonded specimens were subjected to cold and heat cycles (5 C and 55 C, 2500 cycles) and enzymatic hydrolysis (3 weeks, 37 C). The tensile section of dentin segment was observed by scanning electron microscopy. Two intact and unbroken resin-dentin bonding specimens were examined by scanning electron microscopy. Results The collagen of mussel adhesive protein group, GM6001 group and distilled water group were detected by scanning electron microscopy. The activity of enzymes (nmol / min / mg) was 20.22 (+ 0.93), 29.11 (+ 1.17) and 31.39 (+ 0.52), respectively. there were statistical differences among the three groups (p0.01). the degradation of dentin collagen (hydroxyproline release amount (ug / ml) was 2.70 (+ 0.53), 4.00 (+ 1.19) and 5.40 (+ 1.00), respectively. There was no significant difference among the three groups (p0.01). The results of scanning electron microscopy (SEM) were consistent with the above results. Immediate bonding interface scan showed that collagen fibers rarely exposed in the mixed layer of mussel adhesive protein group. A small amount of collagen fibers were found in GM6001 group and distilled water group. Scanning results showed that collagen fibers were less exposed in mussel adhesin group and GM6001 group than in distilled water group, and there were larger gaps in resin-processed dentin tubules in distilled water group. The results showed that most of the tensile sections of the mussel adhesin group and GM6001 group were located at the top of the mixed layer, and the dentinal tubules were obstructed by resin process, while those of the distilled water group were mostly located at the base of the mixed layer, and a large number of dentinal tubules were empty. It is expected that the durability of resin dentin bonding will be improved.
【學位授予單位】:安徽醫(yī)科大學
【學位級別】:碩士
【學位授予年份】:2017
【分類號】:R783.1
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