Table 1.
The thermal stabilities, binding affinities, and anticoagulant effects of TBA variants
| Mutant | Tm (°C) | KD (nM) | t (min) | Mutant | Tm (°C) | Kd (nM) | t (min) |
|---|---|---|---|---|---|---|---|
| TBA | 50.7 | 20.2 ± 1.3 | 4.81 | ||||
| 3Ala | 50.9 | 21.4 ± 2.8 | 3.67 | 12Ala | 51.7 | 51.0 ± 3.8 | 2.74 |
| 3Trp | 54.5 | >140 | 2.89 | 12Trp | 54.7 | 67.3 ± 12.1 | 3.12 |
| 3Leu | 54.3 | 10.9 ± 0.2 | 4.15 | 12Leu | 53.6 | 72.2 ± 0.9 | 4.14 |
| 3Ser | 51.7 | 14.6 ± 0.3 | 2.51 | 12Ser | 52.0 | 86.6 ± 4.5 | 2.34 |
| 3Phe | 54.3 | 22.6 ± 4.8 | 3.39 | 12Phe | 54.3 | 99.1 ± 6.3 | 4.07 |
| 3Amide | 52.6 | 29.2 ± 0.4 | 4.17 | 12Amide | 51.2 | 30.6 ± 6.1 | 3.97 |
| 3Bz | 52.3 | 30.0 ± 6.6 | 4.54 | 12Bz | 54.4 | >200 | 4.08 |
| 3NB | 51.7 | 163.5 ± 3.5 | 3.82 | 12NB | 53.1 | >200 | 3.60 |
| 3Nic | 52.1 | 27.1 ± 4.2 | 3.69 | 12Nic | 52.5 | >200 | 3.56 |
| 3G | 52.9 | 9.8 ± 0.6 | 3.34 | 12G | 53.4 | 20.7 ± 2.8 | 2.88 |
| 3L | 51.5 | 11.6 ± 0.5 | 5.28 | 12L | 51.0 | 27.2 ± 3.0 | 4.17 |
Tm was measured in 100 mM KCl; KD was measured in 100 mM potassium phosphate; t is the time required to reach 30% of the absorbance maximum at 360 nm; t = 0.87 min was observed for the blank sample (without aptamer). The errors in the Tm and t values were within 0.5°C and 0.1 min, respectively.