Unbinding of the streptavidin-biotin complex by atomic force microscopy: a hybrid simulation study.
Unbinding of the streptavidin-biotin complex by atomic force microscopy: a hybrid simulation study.
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DOI：
10.1063/1.2337629
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发表时间：
2006-09
期刊：
影响因子：
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通讯作者：
Jian Zhou;Luzheng Zhang;Y. Leng;H. Tsao;Yu-Jane Sheng;Shaoyi Jiang
中科院分区：
文献类型：
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作者：
Jian Zhou;Luzheng Zhang;Y. Leng;H. Tsao;Yu-Jane Sheng;Shaoyi Jiang
采用分子动力学和连续介质力学相结合的混合分子模拟技术，研究了链霉亲和素-生物素复合物的单分子解结合力。这种混合方法能够在原子力显微镜（AFM）实验的毫秒时间尺度上对解绑定事件进行原子模拟。在AFM实验中，链霉亲和素-生物素复合物的解结合力与加载速率（悬臂弹簧常数与拉力速度的乘积）呈对数关系。分析了解束缚力、悬臂和尖端位置、能垒位置和解束缚途径。本工作的混合模拟结果不仅解释了非结合AFM实验，而且提供了AFM实验中无法获得的详细分子信息。
A hybrid molecular simulation technique, which combines molecular dynamics and continuum mechanics, was used to study the single-molecule unbinding force of a streptavidin-biotin complex. The hybrid method enables atomistic simulations of unbinding events at the millisecond time scale of atomic force microscopy (AFM) experiments. The logarithmic relationship between the unbinding force of the streptavidin-biotin complex and the loading rate (the product of cantilever spring constant and pulling velocity) in AFM experiments was confirmed by hybrid simulations. The unbinding forces, cantilever and tip positions, locations of energy barriers, and unbinding pathway were analyzed. Hybrid simulation results from this work not only interpret unbinding AFM experiments but also provide detailed molecular information not available in AFM experiments.