Table 2.
Summary of the kinetic properties of S100B binding to p53, TRTK12, NDR, HDM2 and HDM4 and determined using NMR and ITC experiments and LineShapeKin analysis.
| Peptide | Kd, App (μM)a | Koff (s-1) | Kon (1×107 M-1 s-1) |
|---|---|---|---|
| TRTK12 | 2 ± 0.5 | 110 ± 20 | 5 ± 2 |
| p53, low salt | 2 ± 0.5 | 760 ± 150 | 40 ± 16 |
| p53, high salt | 30 ± 6 | 900 ± 180 | 3 ± 1 |
| NDR | 0.4 ± 0.2, 2 ± 1b | 50-250, 20-200 b | 13-63, 1-10b |
| HDM2 | 0.5 ± 0.2c | 140 ± 30 | 30 ± 11 |
| HDM4 | 0.07 ± 0.03c | 30 ± 10 | 4 ± 2 |
a
Peptide binding was fit to a single site model for all peptides during the LineShapeKin analysis. All reported values are for the apparent Kd.
b
Kinetic rates could not be solved for analytically. See Materials and Methods.
c
Binding model used was one peptide per S100B dimer. Kd value was taken from ITC and Koff was floated.