TY - JOUR
T1 - Excimer formation dynamics of intramolecular π-stacked perylenediimides probed by single-molecule fluorescence spectroscopy
AU - Yoo, Hyejin
AU - Yang, Jaesung
AU - Yousef, Andrew
AU - Wasielewski, Michael R.
AU - Kim, Dongho
PY - 2010/3/24
Y1 - 2010/3/24
N2 - π-Stacked perylenedlimldes (PDIs) have strong electronic communication between the individual molecules and show great promise as organic electronic materials for applications In field effect transistors, photovoltaics, and liquid crystal displays, To gain further insight into the relationship between conformational behaviors and electronic structures of π-stacked PDIs, we have investigated changes in the excimer-like state of cofacial PDI ollgomers that result from π-stacklng In real time by monitoring the single-molecule fluorescence intensity and lifetime trajectories In a PMMA polymer matrix, The fluorescence intensity and lifetime of π-stacked perylenediimides are sensitive to the degree of π -orbital interactions among PDI units, which is strongly associated with molecular conformations in the polymer matrix. Furthermore, our results can be applied to probe the conformational motions of biomolecules such as proteins.
AB - π-Stacked perylenedlimldes (PDIs) have strong electronic communication between the individual molecules and show great promise as organic electronic materials for applications In field effect transistors, photovoltaics, and liquid crystal displays, To gain further insight into the relationship between conformational behaviors and electronic structures of π-stacked PDIs, we have investigated changes in the excimer-like state of cofacial PDI ollgomers that result from π-stacklng In real time by monitoring the single-molecule fluorescence intensity and lifetime trajectories In a PMMA polymer matrix, The fluorescence intensity and lifetime of π-stacked perylenediimides are sensitive to the degree of π -orbital interactions among PDI units, which is strongly associated with molecular conformations in the polymer matrix. Furthermore, our results can be applied to probe the conformational motions of biomolecules such as proteins.
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U2 - 10.1021/ja910724x
DO - 10.1021/ja910724x
M3 - Article
C2 - 20184367
AN - SCOPUS:77949816792
SN - 0002-7863
VL - 132
SP - 3939
EP - 3944
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
IS - 11
ER -