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Inhibition of Beta‐Amyloid Peptide Aggregation by Multifunctional Carbazole‐Based Fluorophores
Author(s) -
Yang Wanggui,
Wong Yi,
Ng Olivia T. W.,
Bai LiPing,
Kwong Daniel W. J.,
Ke Ya,
Jiang ZhiHong,
Li HungWing,
Yung Ken K. L.,
Wong Man Shing
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201104150
Subject(s) - cyanine , fibrillogenesis , carbazole , peptide , chemistry , biophysics , amyloid (mycology) , amyloid beta , alzheimer's disease , combinatorial chemistry , fibril , biochemistry , fluorescence , photochemistry , disease , medicine , biology , inorganic chemistry , physics , quantum mechanics
Stopping aggregation : Carbazole‐based cyanine fluorophores bind selectively to the Aβ (1–40) peptide and its aggregates which are responsible for causing Alzheimer's disease. One of these fluorophores, SLOH, exerts a strong inhibitory effect on Aβ (1–40) fibrillogenesis (see scheme) and can pass through the blood‐brain barrier making it a potential therapeutic agent for Alzheimer's disease.