TY - JOUR
T1 - Probing Single Molecule Binding and Free Energy Profile with Plasmonic Imaging of Nanoparticles
AU - Wang, Hui
AU - Tang, Zhuodong
AU - Wang, Yan
AU - Ma, Guangzhong
AU - Tao, Nongjian
N1 - Funding Information:
We thank Wei Wei for SEM measurement. Financial support of this work from National Natural Science Foundation of China (NSFC, Grants 21773117, 21904062, and 21575062) is acknowledged.
Publisher Copyright:
Copyright © 2019 American Chemical Society.
PY - 2019/10/9
Y1 - 2019/10/9
N2 - Measuring binding between molecules is critical for understanding basic biochemical processes, developing molecular diagnosis, and screening drugs. Here we study molecular binding at the single molecule level by attaching nanoparticles to the molecular binding pairs. We track the thermal fluctuations of the individual nanoparticles with sub-nanometer precision using a plasmonic scattering imaging technique and show that the fluctuations are controlled by the molecular binding pairs rather than by the nanoparticles. Analysis of the thermal fluctuations provides unique information on molecular binding, including binding energy profile, effective spring constant, and switching between single and multiple molecular binding events. The method provides new insights into molecular binding and also allows one to differentiate nonspecific binding from specific binding, which has been a difficult task in biosensors.
AB - Measuring binding between molecules is critical for understanding basic biochemical processes, developing molecular diagnosis, and screening drugs. Here we study molecular binding at the single molecule level by attaching nanoparticles to the molecular binding pairs. We track the thermal fluctuations of the individual nanoparticles with sub-nanometer precision using a plasmonic scattering imaging technique and show that the fluctuations are controlled by the molecular binding pairs rather than by the nanoparticles. Analysis of the thermal fluctuations provides unique information on molecular binding, including binding energy profile, effective spring constant, and switching between single and multiple molecular binding events. The method provides new insights into molecular binding and also allows one to differentiate nonspecific binding from specific binding, which has been a difficult task in biosensors.
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U2 - 10.1021/jacs.9b08405
DO - 10.1021/jacs.9b08405
M3 - Article
C2 - 31525042
AN - SCOPUS:85072961302
SN - 0002-7863
VL - 141
SP - 16071
EP - 16078
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
IS - 40
ER -