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ABSTRACT: Background and purpose
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.Experimental approach
We developed a specific and quantitative time-resolved FRET (TR-FRET)-based binding assay for Aβ to α7nAChR and pharmacologically characterized t
SUBMITTER: Cecon E
PROVIDER: S-EPMC6715828 | biostudies-literature | 2019 Sep
REPOSITORIES: biostudies-literature