Table 3.
Kinetic parameters and affinity determination of VNAR-Fcs binding to human ICOSL.
| VNAR-Fc | ka (1/Ms) | kd (1/s) | KD (M) |
|---|---|---|---|
| VNAR 1 | 3.11 × 105 | 9.51 × 10−4 | 3.06 × 10−9 |
| VNAR 2 | 5.50 × 105 | 6.69 × 10−4 | 1.22 × 10−9 |
| VNAR 3 | 5.96 × 105 | 1.00 × 10−3 | 1.68 × 10−9 |
| VNAR 4 | 8.73 × 105 | 3.93 × 10−3 | 4.50 × 10−9 |
| VNAR 5 | 3.73 × 105 | 4.15 × 10−3 | 1.11 × 10−8 |
| VNAR 6 | 3.26 × 105 | 2.73 × 10−3 | 8.39 × 10−9 |
| Isotype control 2V | Did not bind |
Kinetic measurements of anti-huICOSL domains. Kinetic analysis of six anti-huICOSL lead domains is summarized in the table. The interaction between the lead clones and huICOSL was measured by surface plasmon resonance (SPR). An anti-human IgG antibody was immobilized on a Biacore chip and the VNAR clones captured via their Fc region.
ka—association rate constant; kd—dissociation rate constant; KD—binding affinity.