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September 27, 2025Open Access

Accurate Prediction of Drug Resistance for Intrinsically Disordered Protein Regions

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Authors

AKAudrius KalpokasMMMark MackeyJMJulien Michel

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Overview

Research demonstrates enhanced binding affinity predictions for MDM2 mutations, highlighting pivotal FEP protocols.

Key Points

  • Equilibrium free energy perturbation protocols significantly improve binding affinity predictions for MDM2 mutations.
  • Binding affinities of MDM2 mutants were assessed against ligands AM-7209 and Nutlin-3a using advanced FEP techniques.
  • The protein force field and water model significantly influence the simulation accuracy in intrinsically disordered regions.
  • Systematic evaluation reveals that predicted values from the equilibrium protocol closely align with experimental data.

Cite This Study

Kalpokas et al. (2025) studied this question.

synapsesocial.com/papers/68d7b3d4eebfec0fc5236357https://doi.org/10.26434/chemrxiv-2025-brzks
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Accurate Prediction of Drug Resistance for Intrinsically Disordered Protein Regions2025
  2. 2Comparison of Methodologies for Absolute Binding Free Energy Calculations of Ligands to Intrinsically Disordered Proteins2024 · 1 citations
  3. 3Robust prediction of relative binding energies for protein-protein complex mutations using free energy perturbation calculations2024 · 4 citations
  4. 4Molecular driving force of a small molecule-induced protein disorder-order transition2026
  5. 5Accurate predictions of protein mutational effects accelerated with a hybrid-topology free energy protocol2025