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Lee, Chang Young
Carbon Nanomaterials Lab
Research Interests
  • Carbon nanomaterials, gas sensors, neuroanalytical chemistry, biomimetic nanosystems

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

Cited 12 times inthomson ciCited 11 times inthomson ci
Title
Single-Molecule Recognition of Biomolecular Interaction via Kelvin Probe Force Microscopy
Other Titles
Single-Molecule Recognition of Biomolecular Interaction via Kelvin Probe Force Microscopy
Author
Park, JinsungYang, JaemoonLee, GyudoLee, Chang YoungNa, SungsooLee, Sang WooHaam, SeungjooHuh, Yong-MinYoon, Dae SungEom, KilhoKwon, Taeyun
Keywords
single molecule; biomolecular interactions; protein kinase; Kelvin probe force microscopy; label-free; surface potential
Issue Date
201109
Publisher
AMER CHEMICAL SOC
Citation
ACS NANO, v.5, no.9, pp.6981 - 6990
Abstract
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
URI
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DOI
http://dx.doi.org/10.1021/nn201540c
ISSN
1936-0851
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