Table 1 K_d and thermodynamic parameters of inhibitor binding to MPro^WT and MPro^D48Y/ΔP168

Inhibitor	K_d-fold increase	1/K_a (µM)	ΔH, kcal/mol	ΔS, cal/mol/K	ΔG, kcal/mol	ΔT_m (°C)
MPro^WT + GC373	1	0.15 ± 0.03	−6.7 ± 0.10	9.1	−9.4	19.8
MPro^D48Y/ΔP168 + GC373	0.9	0.14 ± 0.02	−9.1 ± 0.10	1.27	−9.4	21.1
MPro^WT + NMV	1	0.007 ± 0.003	–10.8 ± 0.70	1.57	–11.2	21.1
MPro^D48Y/ΔP168 + NMV	3	0.018 ± 0.009	−9.5 ± 0.1	3.74	−10.7	22.3
MPro^WT + ESV	1	0.006 ± 0.003	−15.4 ± 0.01	−13.9	−11.2	18.9
MPro^D48Y/ΔP168 + ESV	5	0.028 ± 0.007	−12.2 ± 0.01	−6.01	−10.4	17.8

Titrations were carried out in buffer B at 28 °C with 30 µM protein in the cell and inhibitor (in the syringe) at 10 times the protein concentration. Previous ITC results of MPro^WT with the corresponding inhibitors are included for ease of comparison^14,18,36,47. ΔT_m denotes the difference in T_m measured in the presence and absence of inhibitor (Fig. 2C).

Quick links

Search