What question did this study set out to answer?

The aim is to understand how mutations affect the effectiveness of the SARS-CoV-2 Mpro inhibitor WU-04.

Mutation-Induced Resistance of SARS-CoV-2 Mpro to WU-04 Revealed by Multi-Scale Modeling

View Full Paper

Ask AI

Bookmark

Authors

Reveals changes in binding affinity and structural dynamics in SARS-CoV-2, suggesting ways to create more effective inhibitors.

The aim is to understand how mutations affect the effectiveness of the SARS-CoV-2 Mpro inhibitor WU-04.
Conducted multi-scale molecular dynamics simulations over microsecond scales.
Evaluated binding affinities of wild type and various mutant proteases.
Applied network-rewiring inference to analyze communication pathways in the protease.
Single mutations reduced binding affinity by up to ~12 kcal/mol.
The double mutant M49K/S301P restored engagement with WU-04.
Network analysis showed that residue 301 affects communication between protein domains.

Liu et al. (2026) studied this question.

View Full Paper

Ask AI

Bookmark

View Full Paper

Ask AI

Bookmark

Authors

Reveals changes in binding affinity and structural dynamics in SARS-CoV-2, suggesting ways to create more effective inhibitors.

The aim is to understand how mutations affect the effectiveness of the SARS-CoV-2 Mpro inhibitor WU-04.
Conducted multi-scale molecular dynamics simulations over microsecond scales.
Evaluated binding affinities of wild type and various mutant proteases.
Applied network-rewiring inference to analyze communication pathways in the protease.
Single mutations reduced binding affinity by up to ~12 kcal/mol.
The double mutant M49K/S301P restored engagement with WU-04.
Network analysis showed that residue 301 affects communication between protein domains.

Liu et al. (2026) studied this question.

View Full Paper

Ask AI

Bookmark