Boix Marcel, Eslava Salvador, Costa Machado Gil, Gosselin Emmanuel, Ni Na, Saiz Eduardo, De Coninck Joël
Université De Mons-UMONS, Laboratoire De Physique Des Surfaces Et Des Interfaces, Avenue Maistriau 19, Mons, 7000, Belgium.
Department of Chemical Engineering, University of Bath, United Kingdom.
J Biomed Mater Res A. 2015 Nov;103(11):3493-502. doi: 10.1002/jbm.a.35496. Epub 2015 May 19.
Arthritis, bone fracture, bone tumors and other musculoskeletal diseases affect millions of people across the world. Nowadays, inert and bioactive ceramics are used as bone substitutes or for bone regeneration. Their bioactivity is very much dictated by the way proteins adsorb on their surface. In this work, we compared the adsorption of albumin and fibrinogen on inert and calcium phosphates ceramics (CaPs) using attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR) to follow in situ protein adsorption on these materials. To this effect, we developed a sol-gel technique to control the surface chemistry of an ATR-FTIR detector. Hydroxyapatite adsorbed more albumin and β-tricalcium phosphate adsorbed more fibrinogen. Biphasic calcium phosphate presented the lowest adsorption among CaP for both proteins, illustrating the effect of surface heterogeneities. Inert ceramics adsorbed a lower amount of both proteins compared with bioactive ceramics. A significant change was observed in the conformation of the adsorbed protein versus the surface chemistry. Hydroxyapatite produced a larger loss of α-helix structure on albumin and biphasic calcium phosphate reduced β-sheet percentage on fibrinogen. Inert ceramics produced large α-helix loss on albumin and presented weak interaction with fibrinogen. Zirconia did not adsorb albumin and titanium dioxide promoted huge denaturalization of fibrinogen.
关节炎、骨折、骨肿瘤和其他肌肉骨骼疾病影响着全球数百万人。如今,惰性和生物活性陶瓷被用作骨替代物或用于骨再生。它们的生物活性在很大程度上取决于蛋白质在其表面的吸附方式。在这项工作中,我们使用衰减全反射傅里叶变换红外光谱(ATR-FTIR)比较了白蛋白和纤维蛋白原在惰性陶瓷和磷酸钙陶瓷(CaPs)上的吸附情况,以原位跟踪这些材料上的蛋白质吸附。为此,我们开发了一种溶胶-凝胶技术来控制ATR-FTIR检测器的表面化学性质。羟基磷灰石吸附的白蛋白更多,β-磷酸三钙吸附的纤维蛋白原更多。在两种蛋白质方面,双相磷酸钙在CaP中吸附量最低,这说明了表面不均匀性的影响。与生物活性陶瓷相比,惰性陶瓷吸附的两种蛋白质数量都较少。观察到吸附蛋白质的构象相对于表面化学性质有显著变化。羟基磷灰石使白蛋白的α-螺旋结构损失更大,双相磷酸钙降低了纤维蛋白原的β-折叠百分比。惰性陶瓷使白蛋白的α-螺旋大量损失,并且与纤维蛋白原的相互作用较弱。氧化锆不吸附白蛋白,二氧化钛促进纤维蛋白原的大量变性。