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. Author manuscript; available in PMC: 2022 Dec 15.
Published in final edited form as: Bioconjug Chem. 2021 Nov 14;32(12):2497–2506. doi: 10.1021/acs.bioconjchem.1c00463

Figure 2.

Figure 2.

Kinetics of RBD binding to hACE2 in solution. (a) Sensorgrams from biolayer interferometry experiments showing RBD at five different concentrations binding to hACE2 immobilized on streptavidin sensors. The RBD concentrations are 202, 404, 605, 809, and 1010 nM, respectively. The experimental traces are shown in black, and the fits are shown in red. (b) Observed rate constant for phase 1 of RBD association with hACE2, kobs,1, follows a linear dependence on [RBD], which is shown by the red fitted line. (c) Observed rate constant for phase 2 of RBD association with hACE2, kobs,2, follows a hyperbolic dependence on [RBD], which is shown by the red fitted curve. (d) Observed rate constant for RBD dissociation from hACE2, kobs,dissociation, within error, is independent of [RBD]. The red straight line indicates the mean value of the dissociation rate. For (b–d), error bars represent the standard error from exponential fits of individual traces shown in (a). The quantitative data are representative of three independent repeats of the same experiments.