journal menu
![[Figure 3]](ni5021fig3mag.jpg)
|
|
Figure 3
Indirect assessment of the Q498Y substitution in the binding affinity to ACE2. (a) ACE2 at a concentration of 400 nM, either free (blue line) or pre-incubated in solution with 400 nM RBD wt, RBD Q498Y or RBD β, was loaded over the RBD wt-coated surface and the binding profile was monitored. (b) Inhibition of the coated SARS-CoV-2 RBD wt–ACE2 interaction by soluble RBD wt, RBD Q498Y or RBD β measured by neutralization in an ELISA-like plate assay. The graph shows the reduction of ACE2 binding to surface-immobilized RBD as the concentration of competitor in solution increases. Binding is measured as the absorbance at 450 nm (y axis) and is plotted against the concentration of each competitor (x axis). Each point represents mean absorbance percentage values ± standard deviation (SD). Normalized absorbance values (with 0% being the lowest value and 100% being the highest) were fitted to a concentration of inhibitor versus normalized response equation using GraphPad Prism 9.0 to obtain the curves and calculate the IC50 values for each tested RBD. |
![[Figure 3]](ni5021fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
Open 
access
access
