A bottom-up approach to understanding protein layer formation at solid-liquid interfaces.

A bottom-up approach to understanding protein layer formation at solid-liquid interfaces.
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DOI:
10.1016/j.cis.2013.12.006
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发表时间:
2014-05
影响因子:
15.6
通讯作者:
Schwartz DK
Schwartz DK
中科院分区:
化学1区
文献类型:
--
作者:
Kastantin M;Langdon BB;Schwartz DK

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不同领域(例如分离、生物传感器、生物材料、制药)的共同目标是了解蛋白质在固液界面的行为如何受到环境条件的影响。在许多因素中,温度、pH、离子强度以及固体表面的化学和物理性质可以控制微观蛋白质动力学(例如吸附、解吸、扩散、聚集),其有助于宏观性质,如时间依赖性总蛋白质表面覆盖率和蛋白质结构。这些关系通常通过自上而下的方法进行研究,其中宏观观察使用基于合理但不普遍正确的分析模型来解释,简化了对微观蛋白质动力学的假设。将微观动力学与环境因素联系起来的结论可能会因潜在的不正确假设而产生严重偏差。相比之下,更复杂的模型避免了几个常见的假设,但需要许多参数,这些参数对宏观平均蛋白质性质的预测有重叠的影响。因此,这些模型不太适合自上而下的方法。由于这些模型的复杂性最终可能被证明是理解界面蛋白质行为的关键,本文提出了一种自下而上的方法,其中微观蛋白质动力学的直接观察指定复杂模型中的参数,然后生成宏观预测与实验进行比较。在这个框架中,单分子跟踪已被证明能够直接测量微观蛋白质动力学,但必须通过建模来补充,以联合收割机并将许多独立的微观观察外推到宏观尺度。预计自下而上的方法将更好地将环境因素与宏观蛋白质行为联系起来,从而指导促进理想蛋白质行为的理性选择。
A common goal across different fields (e.g. separations, biosensors, biomaterials, pharmaceuticals) is to understand how protein behavior at solid-liquid interfaces is affected by environmental conditions. Temperature, pH, ionic strength, and the chemical and physical properties of the solid surface, among many factors, can control microscopic protein dynamics (e.g. adsorption, desorption, diffusion, aggregation) that contribute to macroscopic properties like time-dependent total protein surface coverage and protein structure. These relationships are typically studied through a top-down approach in which macroscopic observations are explained using analytical models that are based upon reasonable, but not universally true, simplifying assumptions about microscopic protein dynamics. Conclusions connecting microscopic dynamics to environmental factors can be heavily biased by potentially incorrect assumptions. In contrast, more complicated models avoid several of the common assumptions but require many parameters that have overlapping effects on predictions of macroscopic, average protein properties. Consequently, these models are poorly suited for the top-down approach. Because the sophistication incorporated into these models may ultimately prove essential to understanding interfacial protein behavior, this article proposes a bottom-up approach in which direct observations of microscopic protein dynamics specify parameters in complicated models, which then generate macroscopic predictions to compare with experiment. In this framework, single-molecule tracking has proven capable of making direct measurements of microscopic protein dynamics, but must be complemented by modeling to combine and extrapolate many independent microscopic observations to the macro-scale. The bottom-up approach is expected to better connect environmental factors to macroscopic protein behavior, thereby guiding rational choices that promote desirable protein behaviors.
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