Effects of surface wettability and contact time on protein adhesion to biomaterial surfaces
Effects of surface wettability and contact time on protein adhesion to biomaterial surfaces
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DOI：
10.1016/j.biomaterials.2007.03.032
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发表时间：
2007-08-01
期刊：
影响因子：
14
通讯作者：
Siedlecki, Christopher A.
中科院分区：
文献类型：
--
作者：
Xu, Li-Chong;Siedlecki, Christopher A.
使用原子力显微镜 (AFNI) 直接测量三种测试蛋白质与经辉光放电等离子体处理以产生不同水平的水润湿性的低密度聚乙烯 (LDPE) 表面之间的粘附力。蛋白质对 LDPE 基材的粘附显示出对表面润湿性的阶跃依赖性（通过水接触角 (theta) 测量）。对于 θ >-60-65 度的 LDPE 表面，观察到牛血清白蛋白、纤维蛋白原和人 FXII 的粘附力比 θ < 60 度的表面更强。尽管趋势相同，但在所有表面上观察到 FXII 的粘附力比其他两种蛋白质更小。将每种蛋白质-表面组合的接触时间从 0 秒增加到 50 秒，无论表面润湿性如何，都会增加粘附力。将随时间变化的粘附数据拟合至指数模型并计算蛋白质展开的自由能。根据之前发表的研究，该数据表明蛋白质变性的两步模型，早期阶段为数秒到几分钟，其中蛋白质的外表面与基质相互作用，第二阶段涉及疏水性氨基酸从蛋白质核心到蛋白质/表面界面的移动。影响陈述：本手稿中描述的工作显示了在水接触角 60-65 度范围内蛋白质粘附和蛋白质非粘附材料之间的明显转变，这与蛋白质吸附的已知变化一致和活动。粘附力随时间的变化用于计算与蛋白质-表面相互作用相关的展开能量。该分析为表面蛋白质变性的两步模型提供了理由。 (c) 2007 Elsevier Ltd. 保留所有权利。
Atomic force microscopy (AFNI) was used to directly measure the adhesion forces between three test proteins and low density polyethylene (LDPE) surfaces treated by glow discharge plasma to yield various levels of water wettability. The adhesion of proteins to the LDPE substrates showed a step dependence on the wettability of surfaces as measured by the water contact angle (theta). For LDPE surfaces with theta >-60-65 degrees, stronger adhesion forces were observed for bovine serum albumin, fibrinogen and human FXII than for the surfaces with theta < 60 degrees. Smaller adhesion forces were observed for FXII than for the other two proteins on all surfaces although trends were identical. Increasing the contact time from 0 to 50 s for each protein-surface combination increased the adhesion force regardless of surface wettability. Time varying adhesion data was fit to an exponential model and free energies of protein unfolding were calculated. This data, viewed in light of previously published studies, suggests a 2-step model of protein denaturation, an early stage on the order of seconds to minutes where the outer surface of the protein interacts with the substrate and a second stage involving movement of hydrophobic amino acids from the protein core to the protein/surface interface.Impact statement: The work described in this manuscript shows a stark transition between protein adherent and protein non-adherent materials in the range of water contact angles 60-65 degrees, consistent with known changes in protein adsorption and activity. Time-dependent changes in adhesion force were used to calculate unfolding energies relating to protein-surface interactions. This analysis provides justification for a 2-step model of protein denaturation on surfaces. (c) 2007 Elsevier Ltd. All rights reserved.