Table 1.
Kinetic and dissociation constants of LRRC8A-LRR domain-sybody interactions obtained by SPR.
| KD (nM) | kon (mol−1 s−1) | koff (s−1) | ||
|---|---|---|---|---|
| Sb1 | 1 | 24 | 1.25E+06 | 0.030 |
| 2 | 22 | 1.66E+06 | 0.037 | |
| ave. | 23 | 1.5E+06 | 0.034 | |
| Sb2 | 1 | 35 | 8.28E+04 | 0.003 |
| 2 | 60 | 4.99E+04 | 0.003 | |
| ave. | 48 | 6.6E+04 | 0.003 | |
| Sb3 | 1 | 800 | 1.30E+05 | 0.104 |
| 2 | 913 | 1.23E+05 | 0.113 | |
| ave. | 857 | 1.3E+05 | 0.109 | |
| Sb4 | 1 | 27 | ND | ND |
| 2 | 17 | 1.72E+06 | 0.064 | |
| ave. | 22 | - | - | |
| Sb5 | 1 | 175 | 1.14E+06 | 0.199 |
| 2 | 170 | 1.43E+06 | 0.242 | |
| ave. | 173 | 1.3E+06 | 0.221 |
Data were fitted to a single binding site model. Table displays results of two independent biological replicates. Their average is shown in bold (ave.).
The bold values display the average of the two biological replicates.