Beta Amyloid Peptide: Elsinghorst PW, Härtig W, Goldhammer S, Grosche J, Gütschow M: et. al. et.al.et.al.

Elsinghorst PW, Härtig W, Goldhammer S, Grosche J, Gütschow M: et. al. et.al.et.al.


Author of the Paper: Elsinghorst PW, Härtig W, Goldhammer S, Grosche J, Gütschow M.


Title of the Paper: A gorge-spanning, high-affinity cholinesterase inhibitor to explore beta-amyloid plaques.






Journals: Org Biomol Chem. 2009 Oct 7;7(19):3940-6. PubMed Abstract


Address of correspondence: Pharmaceutical Institute, Pharmaceutical Chemistry I, University of Bonn, An der Immenburg 4, D-53121, Bonn, Germany.


Abstract of the Paper


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.



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