Prediction Of The Impact Of Genetic Variability On Drug Sensitivity For Clinically Relevant EGFR Mutations
Surinach, A.; Hospital, A.; Westermaier, Y.; Jorda, L.; Orozco-Ruiz, S.; Beltran, D.; Colizzi, F.; Andrio, P.; Soliva, R.; Municoy, M.; Gelpi, J. L.; Orozco, M.
Show abstract
Mutations in the kinase domain of the Epidermal Growth Factor Receptor (EGFR) can be drivers of cancer and also trigger drug resistance in patients under chemotherapy treatment based on kinase inhibitors use. A priori knowledge of the impact of EGFR variants on drug sensitivity would help to optimize chemotherapy and to design new drugs effective against resistant variants. To this end, we have explored a variety of in silico methods, from sequence-based to state-of-the-art atomistic simulations. We did not find any sequence signal that can provide clues on when a drug-related mutation appears and what will be the impact in drug activity. Low-level simulation methods provide limited qualitative information on regions where mutations are likely to produce alterations in drug activity and can predict around 70% of the impact of mutations on drug efficiency. High-level simulations based on non-equilibrium alchemical free energy calculations show predictive power. The integration of these state-of-the-art methods in a workflow implementing an interface for parallel distribution of the calculations allows its automatic and high-throughput use, even for researchers with moderate experience in molecular simulations.
Matching journals
The top 1 journal accounts for 50% of the predicted probability mass.
Similar papers in this journal
- Rational Prediction of PROTAC-compatible Protein-Protein Interfaces by Molecular Docking 96%
- CANDOCK: Chemical atomic network based hierarchical flexible docking algorithm using generalized statistical potentials 96%
- RosENet: Improving binding affinity prediction by leveraging molecular mechanics energies with a 3D Convolutional Neural Network 96%
Similar papers in this journal
- Reconciling ASPP-p53 Binding Mode Discrepancies through an Ensemble Binding Framework that Bridges Crystallography and NMR Data 95%
- Mechanistic insights into ligand dissociation from the SARS-CoV-2 spike glycoprotein 94%
- Conformational plasticity and dynamic interactions of the N-terminal domain of the chemokine receptor CXCR1 94%
Similar papers in this journal
- Exploring the ability of the MD+FoldX method to predict SARS-CoV-2 antibody escape mutations using large-scale data 95%
- How Communication Pathways Bridge Local and Global Conformations in an IgG4 Antibody: a Molecular Dynamics Study 95%
- Molecular dynamics and in silico mutagenesis on the reversible inhibitor-bound SARS-CoV-2 Main Protease complexes reveal the role of lateral pocket in enhancing the ligand affinity 95%
Similar papers in this journal
- Worth the weight: Sub-Pocket EXplorer (SubPEx), a weighted-ensemble method to enhance binding-pocket conformational sampling 96%
- A benzene-mapping approach for uncovering cryptic pockets in membrane-bound proteins 96%
- Less is more: Coarse-grained integrative modeling of large biomolecular assemblies with HADDOCK 96%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.