Journal: British journal of pharmacology
Article Title: Quantitative assessment of oligomeric amyloid β peptide binding to α7 nicotinic receptor.
doi: 10.1111/bph.14688
Figure Lengend Snippet: FIGURE 3 Effect of well‐characterized compounds on the Aβ/α7nAChR interaction. Competition for Aβ1–42‐FAM binding to Tb‐ SNAP‐α7nAChR by non‐labelled Aβ1–42 (reference, dotted line) and by the compounds (a) S24795 (n = 5), (b) PNU‐282987 (n = 5), (c) EVP‐6124 (n = 5), (d) S65050 (n = 5), (e) anti‐ Aβ antibody (20 μg·ml−1; n = 5), by the α7nAChR type II PAM (f) PNU‐120596 (n = 5) and type I PAM (g) NS1738 (n = 4); (h) model of the α7nAChR homo‐pentamer illustrating the localization of the orthosteric binding site, the proposed allosteric binding sites for NS1738 and PNU‐120596, and the binding site of the channel blocker mecamylamine (adapted from Corradi & Bouzat, 2016; Spurny et al., 2015). All data are expressed as mean ± SEM
Article Snippet: Epibatidine, α‐bungarotoxin, methyllycaconitine, PNU‐282987, PNU‐120596, and NS1738 were purchased from Tocris Bioscience (Bristol, UK).
Techniques: Binding Assay