Power Law Behavior in Protein Desorption Kinetics Originating from Sequential Binding and Unbinding
Power Law Behavior in Protein Desorption Kinetics Originating from Sequential Binding and Unbinding
复制标题
源自顺序结合和解结合的蛋白质解吸动力学中的幂律行为
DOI：
10.1021/acs.langmuir.0c02260
复制
发表时间：
2020
期刊：
影响因子：
3.9
通讯作者：
Katira, Parag
中科院分区：
文献类型：
--
作者：
Armstrong, Megan J.;Rodriguez, Juan B.;Dahl, Peter;Salamon, Peter;Hess, Henry;Katira, Parag
最近在单分子水平上对蛋白质吸附的研究表明，蛋白质的吸附是可逆的，但具有长尾的停留时间分布，该分布可以近似地用与不同吸附位置相关的指数函数和来近似。本文提出，停留时间分布的形状是一个吸附过程的结果，吸附过程具有顺序和可逆的步骤，有助于获得类似于拉链的整体结合强度。在该模型中，单一蛋白质的停留时间分布的生存函数从单一吸附步骤的指数分布到大量吸附步骤的指数−1/2的幂函数分布。用单分子成像技术实验研究了荧光标记的纤维蛋白原在玻璃表面的吸附。该模型能很好地拟合实验停留时间分布。这表明，观察到的长驻留时间可能来自于分步吸附，而不是罕见但强结合部位，并为控制蛋白质在生物材料上的吸附提供了指导。
The study of protein adsorption at the single molecule level has recently revealed that the adsorption is reversible, but with a long-tailed residence time distribution which can be approximated with a sum of exponential functions putatively related to distinct adsorption sites. Here it is proposed that the shape of the residence time distribution results from an adsorption process with sequential and reversible steps that contribute to overall binding strength resembling “zippering”. In this model, the survival function of the residence time distribution of single proteins varies from an exponential distribution for a single adsorption step to a power law distribution with exponent −1/2 for a large number of adsorption steps. The adsorption of fluorescently labeled fibrinogen to glass surfaces is experimentally studied with single molecule imaging. The experimental residence time distribution can be readily fit by the proposed model. This demonstrates that the observed long residence times can arise from stepwise adsorption rather than rare but strong binding sites and provides guidance for the control of protein adsorption to biomaterials.