Protein adsorption in three dimensions.
Protein adsorption in three dimensions.
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DOI：
10.1016/j.biomaterials.2011.10.059
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发表时间：
2012-02
期刊：
影响因子：
14
通讯作者：
Vogler, Erwin A.
中科院分区：
文献类型：
--
作者：
Vogler, Erwin A.
最近的实验和理论工作澄清血液蛋白质吸附的物理化学从水缓冲溶液的各种表面的生物材料应用的背景下，特别是对心血管生物材料的发展进行了审查和解释。通过将“蛋白质吸附问题”简化为三个需要定量回答的核心问题，强调了这一主题在生物材料表面科学中的重要性。对蛋白质吸附文献的概述确定了参与五十多年重点研究的许多研究人员之间不一致的一些来源。蛋白质吸附的基本生物物理化学的教程设置阶段的动力学和热力学的蛋白质吸附的详细讨论，包括两种蛋白质之间的吸附竞争的相同的吸附剂浸在二元蛋白质混合物。动力学和稳态吸附都可以合理化，使用一个单一的解释范式断言，蛋白质分子分区从溶液到一个三维（3D）的界面分离散装溶液从物理吸附剂表面。吸附的蛋白质聚集在一个或多个吸附层中，这取决于蛋白质的大小、溶液浓度和吸附剂表面能（水润湿性）。吸附过程开始于与蛋白质水溶液接触的吸附剂表面的水合。表面水合反应瞬间在吸附剂和蛋白质溶液之间形成薄的伪2D界面。蛋白质分子迅速扩散到这个新形成的界面中，产生一个真正的3D界面，该界面随着到达的蛋白质膨胀，并在mg/mL原液浓度CB下在几毫秒内填充到容量。这种膨胀的界面随后经历了时间依赖性（分钟至小时）的体积VI的减少，通过驱逐界面水和初始吸附的蛋白质。界面蛋白质浓度CI随着VI的降低而增加，导致界面能量的缓慢降低。稳态由净分配系数决定。在占据相间空间的过程中，吸附蛋白质分子必须置换相等体积的相间水。界面水本身通过瞬时氢键网络与表面结合水相关联。因此，相间水的置换需要一定量的能量，该能量取决于吸附剂表面化学/能量。该“吸附-脱水”步骤是吸附的显著自由能成本，其控制在稳定状态下可被吸附到单位吸附剂表面积（吸附剂容量）的蛋白质的最大量。随着吸附剂亲水性增加，蛋白质吸附单调减少，因为表面脱水的能量成本增加，最终导致在以水接触角θ → 65°为特征的吸附剂水润湿性（表面能）附近没有蛋白质吸附。因此，蛋白质不会吸附（在大于本体溶液的相间浓度下积累）到表现出θ < 65°的更亲水的吸附剂。对于具有强刘易斯酸/碱化学性质的吸附剂，例如离子交换树脂，蛋白质/表面相互作用可能是非常有利的，导致蛋白质在相对厚的界面中吸附在多层中。一个简单的，三个组件的自由能关系捕捉蛋白质吸附到所有表面的显著特征，预测蛋白质吸附的总自由能是一个相对较小的倍数的热能的任何表面化学（也许除了生物工程表面承载特定的配体吸附蛋白质），因为表面化学，与蛋白质的化学相互作用也必须通过氢键与水相互作用。以这种方式，水通过与吸附蛋白质分子竞争来缓和蛋白质吸附到任何表面。该主要意见最后提出了对蛋白质吸附范式的几项改变，这些改变可能会推进对构成生物材料表面科学基础的“蛋白质吸附问题”的三个核心问题的回答。
Recent experimental and theoretical work clarifying the physical chemistry of blood-protein adsorption from aqueous-buffer solution to various kinds of surfaces is reviewed and interpreted within the context of biomaterial applications, especially toward development of cardiovascular biomaterials. The importance of this subject in biomaterials surface science is emphasized by reducing the “protein-adsorption problem” to three core questions that require quantitative answer. An overview of the protein-adsorption literature identifies some of the sources of inconsistency among many investigators participating in more than five decades of focused research. A tutorial on the fundamental biophysical chemistry of protein adsorption sets the stage for a detailed discussion of the kinetics and thermodynamics of protein adsorption, including adsorption competition between two proteins for the same adsorbent immersed in a binary-protein mixture. Both kinetics and steady-state adsorption can be rationalized using a single interpretive paradigm asserting that protein molecules partition from solution into a three-dimensional (3D) interphase separating bulk solution from the physical-adsorbent surface. Adsorbed protein collects in one-or-more adsorbed layers, depending on protein size, solution concentration, and adsorbent surface energy (water wettability). The adsorption process begins with the hydration of an adsorbent surface brought into contact with an aqueous-protein solution. Surface hydration reactions instantaneously form a thin, pseudo-2D interface between the adsorbent and protein solution. Protein molecules rapidly diffuse into this newly-formed interface, creating a truly 3D interphase that inflates with arriving proteins and fills to capacity within milliseconds at mg/mL bulk-solution concentrations CB. This inflated interphase subsequently undergoes time-dependent (minutes-to-hours) decrease in volume VI by expulsion of either-or-both interphase water and initially-adsorbed protein. Interphase protein concentration CI increases as VI decreases, resulting in slow reduction in interfacial energetics. Steady-state is governed by a net partition coefficient . In the process of occupying space within the interphase, adsorbing protein molecules must displace an equivalent volume of interphase water. Interphase water is itself associated with surface-bound water through a network of transient hydrogen bonds. Displacement of interphase water thus requires an amount of energy that depends on the adsorbent surface chemistry/energy. This “adsorption-dehydration” step is the significant free-energy cost of adsorption that controls the maximum amount of protein that can be adsorbed at steady state to a unit adsorbent-surface area (the adsorbent capacity). As adsorbent hydrophilicity increases, protein adsorption monotonically decreases because the energetic cost of surface dehydration increases, ultimately leading to no protein adsorption near an adsorbent water wettability (surface energy) characterized by a water contact angle θ → 65°. Consequently, protein does not adsorb (accumulate at interphase concentrations greater than bulk solution) to more hydrophilic adsorbents exhibiting θ < 65° . For adsorbents bearing strong Lewis acid/base chemistry such as ion-exchange resins, protein/surface interactions can be highly favorable, causing protein to adsorb in multilayers in a relatively thick interphase. A straightforward, three-component free energy relationship captures salient features of protein adsorption to all surfaces predicting that the overall free energy of protein adsorption is a relatively small multiple of thermal energy for any surface chemistry (except perhaps for bioengineered surfaces bearing specific ligands for adsorbing protein) because a surface chemistry that interacts chemically with proteins must also interact with water through hydrogen bonding. In this way, water moderates protein adsorption to any surface by competing with adsorbing protein molecules. This Leading Opinion ends by proposing several changes to the protein-adsorption paradigm that might advance answers to the three core questions that frame the “protein-adsorption problem” that is so fundamental to biomaterials surface science.
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DOI：
10.1002/jbm.820030114
发表时间：
1969-03-01
期刊：
Journal of biomedical materials research
影响因子：
--
作者：
Brash, J L;Lyman, D J
通讯作者：
Lyman, D J
DOI：
10.1002/jbm.820180609
发表时间：
1984-01-01
期刊：
JOURNAL OF BIOMEDICAL MATERIALS RESEARCH
影响因子：
--
作者：
BRYNDA, E;CEPALOVA, NA;STOL, M
通讯作者：
STOL, M
影响因子：
3.7
作者：
Anraku, M;Kragh-Hansen, U;Otagiri, M
通讯作者：
Otagiri, M
影响因子：
14
作者：
CASTILLO, EJ;KOENIG, JL;JENTOFT, N
通讯作者：
JENTOFT, N
影响因子：
3.9
作者：
Benjamins, J.;Lyklema, J.;Lucassen-Reynders, E. H.
通讯作者：
Lucassen-Reynders, E. H.