In situ monitoring of single molecule binding reactions with time-lapse atomic force microscopy on functionalized DNA origami

被引:20
作者
Wu, Na [1 ]
Zhou, Xingfei [2 ]
Czajkowsky, Daniel M. [1 ]
Ye, Ming [1 ]
Zeng, Dongdong [1 ]
Fu, Yanming [1 ]
Fan, Chunhai [1 ]
Hu, Jun [1 ]
Li, Bin [1 ]
机构
[1] Chinese Acad Sci, Lab Phys Biol, Shanghai Inst Appl Phys, Shanghai 201800, Peoples R China
[2] Ningbo Univ, Dept Phys, Ningbo 315211, Zhejiang, Peoples R China
关键词
REAL-TIME; BIOTIN BINDING; STREPTAVIDIN; PROTEIN; KINETICS; PLATFORM; AVIDIN; NANOARRAYS; BILAYERS; CRYSTALS;
D O I
10.1039/c1nr10181a
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Individual biomolecular binding events were recorded in situ by combining time-lapse atomic force microscopy and DNA origami. Single streptavidin molecules bound to specifically biotinyated DNA origami were simply counted as a function of time to obtain a direct measure of the binding rate.
引用
收藏
页码:2481 / 2484
页数:4
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