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首页> 外文会议>European corrosion congress;EUROCORR 2009 >Influence of temperature and albumin concentration on the adsorption of bovine Serum Albumin (BSA) on a CoCrMo biomedical alloy
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Influence of temperature and albumin concentration on the adsorption of bovine Serum Albumin (BSA) on a CoCrMo biomedical alloy

机译：温度和白蛋白浓度对CoCrMo生物医学合金吸附牛血清白蛋白（BSA）的影响

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Proteins are relative large biomolecules and have a tendency to accumulate at the interface between solutions and solid surfaces. There has been considered interest in the interfacial behaviour of proteins in the human body as a result of problems associated with bacterial growth and metal dissolution. As consequence of adsorption process on some metal surfaces an accelerated metal ion release rate was obtained; the enhancement of dissolution rate in the presence of proteins can be explained by the formation of biofilm or complexes between metal ions and proteins. Although the biofilm also lubricate the surface, the total material degradation was increased due to increased corrosion.The effects of temperature and BSA concentration on the adsorption mechanisms of BSA adsorption on a CoCrMo biomedical alloy were investigated. Different electrochemical techniques have been employed to characterize the adsorption process, such as Open Circuit Potential measurements (OCP), Electrochemical Impedance Spectroscopy (EIS) and Cyclic Voltammetry (CV). Temperatures selected were extending over the range 298 to 343K and the BSA content was varied between 5 and 500 mg/L in a 0.14M NaCl solution.The effect of protein interaction on the electron transfer processes at the electrode/solution interface was studied using EIS. The charge transfer resistance was very sensitive to the amount of adsorbed protein, indicating that the adsorption process was accompanied by the transfer of charge (via chemisorption) and influenced the mechanism and kinetics of the corrosion reaction. The adsorption process was modelled by the Langmuir isotherm. Thermodynamic parameters of BSA adsorption on CoCrMo surface (ΔG_(Ads), ASads and ΔH_(ADS)) were calculated using the EIS results which also agree with the CV results. Gibbs free energy of adsorption, ΔG_(Ads) values, for BSA (around -51 KJ-mol~(-1)) showed that the molecules have a strong affinity for the CoCrMo surface. Enthalpy and entropy of adsorption suggested that the adsorption process of BSA onto the CoCrMo surface is an endothermic process and the molecule suffers structural changes when adsorbing on the metallic surface.
机译：蛋白质是相对较大的生物分子，并且倾向于在溶液和固体表面之间的界面处积聚。由于与细菌生长和金属溶解有关的问题，人们已经考虑到了蛋白质在人体内的界面行为的兴趣。由于在某些金属表面上进行了吸附过程，因此获得了更快的金属离子释放速率。在蛋白质存在下溶解速度的提高可以通过生物膜或金属离子与蛋白质之间复合物的形成来解释。尽管生物膜也能润滑表面，但是由于腐蚀的增加，总的材料降解也增加了。 研究了温度和BSA浓度对BSA在CoCrMo生物医学合金上吸附机理的影响。已经采用了不同的电化学技术来表征吸附过程，例如开路电势测量（OCP），电化学阻抗谱（EIS）和循环伏安法（CV）。选择的温度范围为298至343K，在0.14M NaCl溶液中BSA含量在5至500 mg / L之间变化。 使用EIS研究了蛋白质相互作用对电极/溶液界面电子转移过程的影响。电荷转移阻力对蛋白质的吸附量非常敏感，表明吸附过程伴随着电荷的转移（通过化学吸附），并影响了腐蚀反应的机理和动力学。吸附过程由Langmuir等温线模拟。使用EIS结果计算了BSA在CoCrMo表面吸附的热力学参数（ΔG_（Ads），ASads和ΔH_（ADS）），该结果也与CV结果一致。牛血清白蛋白的吉布斯吸附自由能，ΔG_（Ads）值（-51 KJ-mol〜（-1））表明该分子对CoCrMo表面具有很强的亲和力。吸附的焓和熵表明，BSA在CoCrMo表面的吸附过程是吸热过程，分子在金属表面吸附时会发生结构变化。

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