Table 1.
Structures and binding affinities (Ki, nM)a of selected compounds screened for nAChR affinity.
| Structure | Compound | α3β4 | α4β2 | α7 |
|---|---|---|---|---|
| Epibatidine | 0.15 ± 0.05 | 0.06 ± 0.0 | 4.16 ± 0.47 | |
| Nicotine | 480.69 ± 59.38 | 11.13 ± 1.11 | ||
| Cytisine | 202.89 ± 18.85 | 1.53 ± 0.20 | ||
| Acetylcholine | 619.63 ± 130.2 | 37.74 ± 3.73 | ||
 |
1 | >10,000 | >10,000 | |
 |
2 | >10,000 | >10,000 | |
 |
3 | >10,000 | >10,000 | |
 |
4 | 2790.3 ± 168.9 | >100,000 | |
 |
5 | 507.86 ± 162.4 | >100,000 | >100,000 |
 |
6 | 421.54 ± 53.43 | >100,000 | |
 |
7 | >10,000 | >10,000 | |
 |
8 | 240.50 ± 29.95 | 10.39 ± 0.21 | |
 |
9 | 2614.78 ± 277 | 423.12 ± 5.90 | |
 |
10 | 169.95 ± 47.91 | 1.95 ± 0.18 | 424 |
 |
11 | 2477.86 ± 123 | 29.31 ± 9.26 | |
 |
12 | 1836.25 ± 210 | >10,000 | |
 |
13 | >10,000 | >10,000 |
a
Binding affinities were determined by inhibition of [3H]epibatidine binding to membranes derived from HEK cells transfected with rat α3β4 and α4β2 nAChR, and rat brain membranes for α7 nAChR.