Effect of pH on stability of dimer structure of the main protease of coronavirus-2.

ABSTRACT: The viral main protease (M^pro) from a novel severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) is a key enzyme essential for viral replication and has become an attractive target for antiviral drug development. The M^pro forms a functional dimer and exhibits a pH-dependent enzyme activity and dimerization. Here, we report a molecular dynamics (MD) investigation to gain insights into the structural stability of the enzyme dimer at neutral and acidic pH. Our data shows larger changes in structure of the protein with the acidic pH than that with the neutral pH. Structural analysis of MD trajectories reveals a substantial increase in intersubunit separation, the loss of domain contacts, binding free energy and interaction energy of the dimer which implies the pro

SUBMITTER: Boonamnaj P 

PROVIDER: S-EPMC9119281 | biostudies-literature | 2022 Aug

REPOSITORIES: biostudies-literature