Thermodynamic data of aptamers binding to adenosine and AMP (at 10 °C).
| Ligands | Aptamers | N | K a (×104 M−1) | K d (μM) | ΔG (kcal mol−1) | ΔH (kcal mol−1) | ΔS (cal K−1 mol−1) |
|---|---|---|---|---|---|---|---|
| Adenosine | One-site Apt | 0.8 ± 0.1 | 35.7 ± 1.4 | 2.8 ± 0.1 | −6.8 ± 1.9 | −13.5 ± 1.9 | −22.4 |
| Res-A10-Right-cut | 0.9 ± 0.2 | 4.8 ± 0.8 | 21.0 ± 3.8 | −5.6 ± 0.3 | −1.1 ± 0.3 | 13.5 | |
| A10-excised Apt | 1.8 ± 0.3 | 6.8 ± 0.9 | 14.8 ± 2.1 | −6.5 ± 0.3 | −1.0 ± 0.3 | 18.7 | |
| AMP | One-site Apt | 1.3 ± 0.3 | 7.39 ± 0.9 | 13.5 ± 1.6 | −6.4 ± 0.8 | −4.5 ± 0.8 | 6.5 |
| Res-A10-Right-cut | —a | ||||||
| A10-excised Apt | —a |
a
Binding was extremely weak and cannot be obtained by ITC.