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. 2018 Oct 18;25(10):1208–1218.e5. doi: 10.1016/j.chembiol.2018.06.012

Table 1.

Binding Characteristics of Fluorescent Ligands Binding to VEGFR2 or NRP1

Fluorescent Ligand Receptor Saturation KD (nM) Kinetic KD (nM) kon (min−1 M−1) koff (min−1)
VEGF165a-TMR NanoLuc-VEGFR2 2.03 ± 0.51 6.64 ± 4.37 1.54 × 107 ± 0.38 × 107 0.06 ± 0.02
VEGF165b-TMR NanoLuc-VEGFR2 9.53 ± 1.36 11.3 ± 3.54 7.29 × 106 ± 1.84 × 106 0.06 ± 0.01
VEGF121a-TMR NanoLuc-VEGFR2 5.54 ± 1.34 5.75 ± 0.46 8.51 × 106 ± 0.81 × 106 0.05 ± 0.00
VEGF165a-TMR NanoLuc-NRP1 4.41 ± 1.34 4.95 ± 1.25 7.11 × 107 ± 2.33 × 107 0.26 ± 0.05

Equilibrium binding parameters for fluorescent VEGF isoforms derived from saturation and kinetic NanoBRET experiments, showing equilibrium dissociation (KD), association rate (kon), and dissociation rate (koff) constants at NanoLuc-VEGFR2 and NanoLuc-NRP1. Data are expressed as mean ± SEM determined from 5 independent experiments.