TY - JOUR
T1 - Aminonaphthalene 2-cyanoacrylate (ANCA) probes fluorescently discriminate between amyloid-β and prion plaques in brain
AU - Cao, Kevin
AU - Farahi, Mona
AU - Dakanali, Marianna
AU - Chang, Willy M.
AU - Sigurdson, Christina J.
AU - Theodorakis, Emmanuel A.
AU - Yang, Jerry
PY - 2012/10/24
Y1 - 2012/10/24
N2 - A major challenge for diagnosing and monitoring the progression of amyloid-based diseases is the capability to distinguish between amyloid deposits that are associated with related, but distinctly different, diseases. Here, we demonstrate that aminonaphthalenyl 2-cyanoacrylate-based probes can fluorescently discriminate between different types of amyloid deposits in brain. The discriminating capability of these molecular rotors is due to the stabilization of the ground versus excited states of these probes as a function of the polarity of their microenvironment (i.e., within the binding pocket on the amyloid). This property makes it possible, for the first time, to estimate the inherent static relative permittivity (ε0) of the binding pocket of each amyloid within tissue. The capability to selectively follow the deposition of specific amyloids in tissue may provide important information for therapeutic development that is not readily accessible from currently available technology.
AB - A major challenge for diagnosing and monitoring the progression of amyloid-based diseases is the capability to distinguish between amyloid deposits that are associated with related, but distinctly different, diseases. Here, we demonstrate that aminonaphthalenyl 2-cyanoacrylate-based probes can fluorescently discriminate between different types of amyloid deposits in brain. The discriminating capability of these molecular rotors is due to the stabilization of the ground versus excited states of these probes as a function of the polarity of their microenvironment (i.e., within the binding pocket on the amyloid). This property makes it possible, for the first time, to estimate the inherent static relative permittivity (ε0) of the binding pocket of each amyloid within tissue. The capability to selectively follow the deposition of specific amyloids in tissue may provide important information for therapeutic development that is not readily accessible from currently available technology.
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U2 - 10.1021/ja3063698
DO - 10.1021/ja3063698
M3 - Article
C2 - 22866977
AN - SCOPUS:84867760555
SN - 0002-7863
VL - 134
SP - 17338
EP - 17341
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
IS - 42
ER -