Probing conformational hotspots for the recognition and intervention of protein complexes by lysine reactivity profiling.

Although the glycyrrhizic acid exhibits significant intervention on the S1 conformation in the local regions of Lys 77 , Lys 129 , Lys 182 , Lys 310 , and Lys 444 ( t -test < 0.05, |δ N LE | ≥ 0.1), we think the S1–ACE2 complex could be still retained as the reactivities of most of the lysine residues at the S1-RBD interaction interface rarely exhibit an increasing trend.

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Interestingly, the N LE value of Lys 444 within the interaction interface of S1-RBD Lys 386 –Lys 462 exhibited further a decreasing trend after the introduction of glycyrrhizic acid into the S1–ACE2 solution ( Fig. 4 ).

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