On the interactions of the receptor-binding domain of SARS-CoV-1 and SARS-CoV-2 spike proteins with monoclonal antibodies and the receptor ACE2

Carolina Corrêa Giron; Aatto Laaksonen; Fernando L. Barroso da Silva

After the proper equilibration of the simulated molecular systems, long production runs were carried out. Simulations whose focus was on titration properties [Z(pH) and pKas] required The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.04.05.026377 doi: bioRxiv preprint that the interface antibody-antigen has a peculiar electrostatic pattern (richer in titratable groups) that is different than other general protein-protein interfaces, 65 etc.]. 27, 55 Such facts contribute to shift the canonical view of the "lock and key" (with a clear focus on the protein surface) to a broader definition that led to the "electrostatic epitopes" (EE) concept. 27 This means that inner titratable groups (not only the ones at the epitope-paratope interface) can also participate in the interplay of interactions with Abs.