Single-Molecule Recognition of Biomolecular Interaction via Kelvin Probe Force Microscopy

被引:55
|
作者
Park, Jinsung [1 ,2 ]
Yang, Jaemoon [1 ,3 ]
Lee, Gyudo [1 ,4 ]
Lee, Chang Young [5 ]
Na, Sungsoo [2 ]
Lee, Sang Woo [4 ]
Haam, Seungjoo [6 ]
Huh, Yong-Min [3 ]
Yoon, Dae Sung [4 ]
Eom, Kilho [1 ,2 ]
Kwon, Taeyun [1 ,4 ]
机构
[1] Inst Mol Sci, Seoul 120749, South Korea
[2] Korea Univ, Dept Mech Engn, Seoul 136701, South Korea
[3] Yonsei Univ, Dept Radiol, Seoul 120752, South Korea
[4] Yonsei Univ, Dept Biomed Engn, Wonju 220740, South Korea
[5] Univ Illinois, Dept Chem, Urbana, IL 61801 USA
[6] Yonsei Univ, Dept Chem & Biomol Engn, Seoul 120749, South Korea
基金
新加坡国家研究基金会;
关键词
single molecule; biomolecular interactions; protein kinase; Kelvin probe force microscopy; label-free; surface potential; LABEL-FREE DETECTION; PROTEIN; BINDING; RESOLUTION; MODELS; CANCER; FIELD; KPFM;
D O I
10.1021/nn201540c
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
We report the scanning probe microscope (SPM)-based single-molecule recognition of biomolecular interactions between protein kinase and small ligands (i.e., ATP and Imatinib). In general, it is difficult to sense and detect the small ligands bound to protein kinase (at single-molecule resolution) using a conventional atomic force microscope (AFM) due to the limited resolution of conventional AFM for detecting the miniscule changes in molecular size driven by ligand binding. In this study, we have demonstrated that Kelvin probe force microscopy. (KPFM) is able to articulate the surface potential of biomolecules interacting with ligands (i.e., the protein kinase-ATP interactions and inhibition phenomena induced by antagonistic molecules) in a label-free manner. Furthermore, measured surface potentials for biomolecular interactions enable quantitative descriptions on the ability of protein kinase to interact with small ligands such as ATP or antagonistic molecules. Our study sheds light on KPFM that allows the precise recognition of single-molecule interactions, which opens a new avenue for the design and development of novel molecular therapeutics.
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页码:6981 / 6990
页数:10
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