Department of Biomaterials , Institute for Bioprocessing and Analytical Measurement Techniques , Rosenhof , D-37308 Heiligenstadt , Germany.
ACS Appl Mater Interfaces. 2018 Dec 12;10(49):42175-42185. doi: 10.1021/acsami.8b17507. Epub 2018 Nov 29.
Although the adsorption of proteins on the Mg surface was ascribed to be the main reason for the effect of proteins on magnesium (Mg) degradation, few studies about the adsorption of proteins on the Mg surface were performed due to the labile circumstances during immersion. In the present study, the adsorption of bovine serum albumin (BSA) and fibrinogen (Fib) on the Mg surface during and after immersion was extensively investigated in different media for the first time. The results revealed that BSA and Fib showed a similar adsorption trend on the Mg surface during and after immersion, and they adsorbed more on the Mg surface in Hank's balanced salt solution (HBSS) than in Dulbecco's modified Eagle medium Glutamax-I (DMEM). The possible influence factors for protein adsorption, such as pH, surface roughness, and wettability, were considered to elucidate different adsorption in HBSS and DMEM. It was found that the participation of Ca in the formation of degradation products largely affected the degradation rate of Mg, changed surface roughness, compactness, and surface charge during immersion, which largely suppressed the adsorption of proteins on the Mg surface.
尽管蛋白质在镁表面的吸附被认为是蛋白质对镁（Mg）降解影响的主要原因，但由于浸泡过程中存在不稳定的情况，很少有关于蛋白质在镁表面吸附的研究。在本研究中，首次在不同介质中广泛研究了牛血清白蛋白（BSA）和纤维蛋白原（Fib）在浸泡过程中和浸泡后的镁表面的吸附情况。结果表明，BSA 和 Fib 在浸泡过程中和浸泡后在镁表面的吸附趋势相似，它们在 Hank's 平衡盐溶液（HBSS）中的吸附量高于在 Dulbecco's modified Eagle medium Glutamax-I（DMEM）中的吸附量。考虑到可能影响蛋白质吸附的因素，如 pH 值、表面粗糙度和润湿性，以阐明在 HBSS 和 DMEM 中吸附的差异。研究发现，Ca 在降解产物形成过程中的参与极大地影响了 Mg 的降解速率，改变了浸泡过程中的表面粗糙度、致密性和表面电荷，这极大地抑制了蛋白质在镁表面的吸附。
