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纤维连接蛋白和骨形态发生蛋白对钛金属生物活性的协同作用。

Synergistic effects of fibronectin and bone morphogenetic protein on the bioactivity of titanium metal.

机构信息

Engineering Research Center in Biomaterials, Sichuan University, Chengdu, Sichuan, 610064, China.

National Engineering Research Center for Biomaterials, Chengdu, Sichuan, 610064, China.

出版信息

J Biomed Mater Res A. 2017 Sep;105(9):2485-2498. doi: 10.1002/jbm.a.36106. Epub 2017 Jun 6.

DOI:10.1002/jbm.a.36106
PMID:28498566
Abstract

To improve the biological properties of bioactive titanium metal, recombinant human bone morphogenetic protein 2(rhBMP-2) and fibronectin (Fn) were adsorbed on its surface solely or contiguously to modify the anodic oxidized titanium (AO-Ti), acid-alkali-treated titanium (AA-Ti), and polished titanium (P-Ti). It is found that the different bioactive titanium surface structures had great influence on protein adsorption. The adsorption amounts of BMP adsorbed solely and Fn/BMP adsorbed contiguously were AA-Ti > P-Ti > AO-Ti, and that for Fn adsorbed solely was AA-Ti ≈ P-Ti > AO-Ti. The conformation of proteins was changed remarkably after the adsorption. For BMP, the α-helix decreased on AA-Ti and stabilized on P-Ti and AO-Ti. For Fn, the β-sheet on PT-Ti and AA-Ti increased significantly. For Fn/BMP, the percentage of β-sheet on AA-Ti increased, and that of α-helix on all samples was stable. MSCs showed greater adhesion and spreading on Fn/BMP groups. MTT and Elisa tests showed that the synergistic effects of proteins made the cells proliferate and differentiate faster. It indicated both the surface structure and the synergistic effects of proteins could influence the biological properties of titanium metals. It provides research foundation for improving the biological properties of bioactive titanium metals by simultaneous application of several proteins. © 2017 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 105A: 2485-2498, 2017.

摘要

为了改善生物活性钛金属的生物学性能,单独或连续地将重组人骨形态发生蛋白 2(rhBMP-2)和纤连蛋白(Fn)吸附在其表面上,以修饰阳极氧化钛(AO-Ti)、酸碱处理钛(AA-Ti)和抛光钛(P-Ti)。结果发现,不同的生物活性钛表面结构对蛋白质吸附有很大的影响。单独吸附的 BMP 和连续吸附的 Fn/BMP 的吸附量为 AA-Ti > P-Ti > AO-Ti,而单独吸附的 Fn 的吸附量为 AA-Ti ≈ P-Ti > AO-Ti。蛋白质的构象在吸附后发生了显著变化。对于 BMP,α-螺旋在 AA-Ti 上减少,在 P-Ti 和 AO-Ti 上稳定。对于 Fn,PT-Ti 和 AA-Ti 上的β-折叠显著增加。对于 Fn/BMP,AA-Ti 上的β-折叠百分比增加,所有样品上的α-螺旋百分比稳定。MSCs 在 Fn/BMP 组上表现出更大的粘附和扩展。MTT 和 Elisa 试验表明,蛋白质的协同作用使细胞更快地增殖和分化。这表明表面结构和蛋白质的协同作用都可以影响钛金属的生物学性能。为通过同时应用几种蛋白质来提高生物活性钛金属的生物学性能提供了研究基础。© 2017 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 105A: 2485-2498, 2017.

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