Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Molecular Dynamics Free Energy Simulations Reveal the Mechanism for the Antiviral Resistance of the M66I HIV-1 Capsid Mutation.

Viruses - 15 May 2021

Sun Qinfang, Levy Ronald M, Kirby Karen A, Wang Zhengqiang, Sarafianos Stefan G, Deng Nanjie

Abstract excerpt

While drug resistance mutations can often be attributed to the loss of direct or solvent-mediated protein-ligand interactions in the drug-mutant complex, in this study we show that a resistance mutation for the picomolar HIV-1 capsid (CA)-targeting antiviral (GS-6207) is mainly due to the free energy cost of the drug-induced protein side chain reorganization in the mutant protein. Among several mutations, M66I...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Anti-HIV Agents
Share to Capsid

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Capsid Proteins

Share to Drug Resistance, Viral

Share to Ligands

Share to Molecular Dynamics Simulation

Share to Protein Conformation

Source

Open in PubMed Open full text

Identifiers

PMID: 34063519
DOI: 10.3390/v13050920
PMCID: PMC8156065

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Molecular Dynamics Free Energy Simulations Reveal the Mechanism for the Antiviral Resistance of the M66I HIV-1 Capsid Mutation.PMID 34063519Read ↗

Some insights into mechanism for binding and drug resistance of wild type and I50V V82A and I84V mutations in HIV-1 protease with GRL-98065 inhibitor from molecular dynamic simulations.Semantic proximity Read ↗

Advanced molecular mechanisms of modified DRV compounds in targeting HIV-1 protease mutations and interrupting monomer dimerization.Semantic proximity Read ↗

Insights into drug resistance of mutations D30N and I50V to HIV-1 protease inhibitor TMC-114: free energy calculation and molecular dynamic simulation.Semantic proximity Read ↗

Multiple Molecular Dynamics Simulations of the Inhibitor GRL-02031 Complex with Wild Type and Mutant HIV-1 Protease Reveal the Binding and Drug-Resistance Mechanism.Semantic proximity Read ↗

Structural and Mechanistic Bases for Resistance of the M66I Capsid Variant to LenacapavirSemantic proximity Read ↗

Drug resistance mechanisms of three mutations V32I, I47V and V82I in HIV-1 protease toward inhibitors probed by molecular dynamics simulations and binding free energy predictionsSemantic proximity Read ↗

Multiple Molecular Dynamics Simulations and Free-Energy Predictions Uncover the Susceptibility of Variants of HIV-1 Protease against Inhibitors Darunavir and KNI-1657.Semantic proximity Read ↗

Structural and mechanistic bases for resistance of the M66I capsid variant to lenacapavir.Semantic proximity Read ↗

Molecular Mechanism of Resistance in a Clinically Significant Double-Mutant Variant of HCV NS3/4A Protease.Semantic proximity Read ↗

Computational Studies of a Mechanism for Binding and Drug Resistance in the Wild Type and Four Mutations of HIV-1 Protease with a GRL-0519 Inhibitor.Semantic proximity Read ↗

Bioactive fungal compounds as potential anti-HIV agents against HIV-1 protease: a multi-faceted molecular modelling approach for drug discovery.Semantic proximity Read ↗

Drug Resistance Mechanism of M46I-Mutation-Induced Saquinavir Resistance in HIV-1 Protease Using Molecular Dynamics Simulation and Binding Energy Calculation.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.