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Quantitative assessment of oligomeric amyloid β peptide binding to α7 nicotinic receptor
Author(s) -
Cecon Erika,
Dam Julie,
Luka Marine,
Gautier Clément,
Chollet AnneMarie,
Delagrange Philippe,
Danober Laurence,
Jockers Ralf
Publication year - 2019
Publication title -
british journal of pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0007-1188
DOI - 10.1111/bph.14688
Subject(s) - allosteric regulation , cholinergic , nicotinic agonist , chemistry , drug discovery , förster resonance energy transfer , binding site , pharmacology , amyloid (mycology) , neuroscience , biochemistry , receptor , biology , fluorescence , inorganic chemistry , physics , quantum mechanics
Progressive dysfunction of cholinergic transmission is a well-known characteristic of Alzheimer's disease (AD). Amyloid β (Aβ) peptide oligomers are known to play a central role in AD and are suggested to impair the function of the cholinergic nicotinic ACh receptor α7 (α7nAChR). However, the mechanism underlying the effect of Aβ on α7nAChR function is not fully understood, limiting the therapeutic exploration of this observation in AD. Here, we aimed to detect and characterize Aβ binding to α7nAChR, including the possibility of interfering with this interaction for therapeutic purposes.