Tuning the translational freedom of DNA for high speed AFM  

作　　者：Andrew J. Lee Michal Szymonik Jamie K. Hobbs Christoph Walti 

机构地区：[1]Bioelectronics, School of Electronic and Electrical Engineering, University of Leeds, Leeds, LS2 9JT, UK [2]Department of Physics and Astronomy, University of Sheffield, Sheffield, 53 7RH, UK

出　　处：《Nano Research》2015年第6期1811-1821,共11页纳米研究（英文版）

摘　　要：Direct observation is arguably the preferred way to investigate the interactions between two molecular complexes. With the development of high speed atomic force microscopy （AFM）, it is becoming possible to observe directly DNA-protein interactions with relevant spatial and temporal resolutions. These interactions are of central importance to biology, bionanotechnology, and functional biologically inspired materials. As in all microscopy studies, sample preparation plays a central role in AFM observation and minimal perturbation of the sample is desired. Here, we demonstrate the ability to tune the interactions between DNA molecules and the surface to create an association strong enough to enable high-resolution AFM imaging while also providing sufficient translational freedom to allow the relevant protein-DNA interactions to take place. Furthermore, we describe a quantitative method for measuring DNA mobility, while also determining the individual forces contributing to DNA movement. We found that for a weak surface association, a significant contribution to the movement arises from the interaction of the AFM tip with the DNA. In combination, these methods enable the tuning of the surface translational freedom of DNA molecules to allow the direct study of a wide range of nucleo-protein interactions by high speed atomic force microscopy.直接观察可以证明是调查在二分子的建筑群之间的相互作用的比较喜欢的方法。与高度的发展加速原子力量显微镜学(AFM ) ，直接与相关空间、时间的分辨率观察 DNA 蛋白质相互作用正在变得可能。这些相互作用具有到生物学， bionanotechnology，和功能的生物学上启发的材料的中央重要性。作为在所有显微镜学研究，样品准备在 AFM 观察和样品的最小的不安起一个中央作用被需要。这里，我们表明能力调节在 DNA 分子和表面之间的相互作用创造足够强壮的一个协会当也提供足够的翻译自由允许相关 protein-DNA 相互作用发生时，启用高分辨率的 AFM 成像。而且，我们为测量 DNA 活动性描述一个量的方法，当也决定贡献 DNA 运动的单个力量时。我们发现为一个弱表面协会，对运动的重要贡献从和 DNA 的 AFM 尖端的相互作用产生。在联合，这些方法启用调节表面由高度允许大量核蛋白相互作用的直接学习的分子加速的 DNA 的翻译自由原子力量显微镜学。

关 键 词：high speed atomic forcemicroscopy （HS-AFM） DNA protein BIONANOTECHNOLOGY 

分 类 号：Q513[生物学—生物化学] TB383[一般工业技术—材料科学与工程]