Dynamical regulations of protein-ligand bindings at single molecular level
Dynamical regulations of protein-ligand bindings at single molecular level
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DOI：
10.1016/j.bbrc.2007.02.031
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发表时间：
2007-04-13
影响因子：
3.1
通讯作者：
Sasaki, Yuji C.
中科院分区：
文献类型：
--
作者：
Sagawa, Takuma;Azuma, Takachika;Sasaki, Yuji C.
我们提出了新的定量规则的结合亲和力使用动态单分子检测系统与X射线。在抗原-抗体相互作用的研究中，我们发现抗原结合对单分子结构的波动具有负调控作用。虽然从宏观上理论和实验上已经对配体诱导稳定性的产生策略进行了很好的研究，但我们的动态单分子实验结果是第一次在实时和空间上具有埃精度的观测。认为这些蛋白质结构波动的负调控与结合事件有关。此外，我们阐明了在所观察到的结构波动中抗原结合条件与非结合条件之间的比率与结合亲和力极其相关。这些结果表明，蛋白质-配体相互作用的现象被认为是稳定的状态，可以被定义为在单分子水平上的动力学过程的结果。这种新的量化从埃级结构波动可以应用于各种生物科学和生物技术。(c)2007年爱思唯尔公司All rights reserved.
We present new quantitative regulations of the binding-affinity using dynamical single-molecule detection system with X-rays. In the study of antigen-antibody interactions, we found that structural fluctuations of single-molecules were negatively regulated by antigen-binding. Although strategies to produce ligand-induced stability have been well studied from the macro aspect both theoretically and experimentally, our dynamical single-molecular experimental results are first observations with angstrom accuracy in the real-time and space. It is considered that those negative regulations of protein structural fluctuations with binding event are related to biological functions. In addition, we clarified that ratio between antigen-binding condition and no-binding one in observed structural fluctuations are extremely relative to the binding-affinity. These results indicate that the phenomena of protein-ligand interactions considered as stable states can be defined as results of dynamical processes at the single-molecule level. Such new quantifications from angstrom-level structural fluctuations can be applied to various biological science and biotechnologies. (c) 2007 Elsevier Inc. All rights reserved.