Author: Elsinghorst PW, Härtig W, Goldhammer S, Grosche J, Gütschow M.
Paper Title:
A gorge-spanning, high-affinity cholinesterase inhibitor to explore beta-amyloid plaques.
Journal: Org Biomol Chem. 2009 Oct 7;7(19):3940-6.
Correspondence: Pharmaceutical Institute, Pharmaceutical Chemistry I, University of Bonn, An der Immenburg 4, D-53121, Bonn, Germany.
Abstract
Cholinesterases are involved in the pathological formation of beta-amyloid plaques. To investigate this pathohistological hallmark of Alzheimer's disease we prepared a high-affinity, fluorescent cholinesterase inhibitor. Its fluorescence intensity was significantly enhanced upon binding to cholinesterases. Using this probe, brain samples from mice and humans affected by Alzheimer's disease were successfully analyzed for beta-amyloid plaques. Unexpectedly, it was discovered, by competition experiments, that the compound binds to amyloid structures, rather than to cholinesterases inside of the plaques.
Source
Amyloid beta (Aβ or Abeta) is a peptide of 36–43 amino acids that is processed from the Amyloid precursor protein. While best known as a component of amyloid plaques in association with Alzheimer's disease, evidence has been found that Aβ is a highly multifunctional peptide with significant non-pathological activity.[1] Aβ is the main component of deposits found in the brains of patients with Alzheimer's disease
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