Evidence map›Paper›PMID 29119352›Full record

ArticleJournal of computer-aided molecular design2018

Using physics-based pose predictions and free energy perturbation calculations to predict binding poses and relative binding affinities for FXR ligands in the D3R Grand Challenge 2.

Christina Athanasiou, Sofia Vasilakaki, Dimitris Dellis, Zoe Cournia

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Article in Journal of computer-aided molecular design, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

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0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

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3 · Its place in the literature

Who cites it

11 citing papers in PubMed.

  1. Article
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  3. Review
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  6. Review
  7. Machine learning classification can reduce false positives in structure-based virtual screening.Proceedings of the National Academy of Sciences of the United States of America · 2020
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4 · The record

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5 · Who and what money

Authors and funding

4 authors.

Christina AthanasiouBiomedical Research Foundation, Academy of Athens, 4 Soranou Ephessiou, 115 27, Athens, Greece.ORCID 0000-0003-2973-3550
Sofia VasilakakiBiomedical Research Foundation, Academy of Athens, 4 Soranou Ephessiou, 115 27, Athens, Greece.ORCID 0000-0002-1008-7264
Dimitris DellisGreek Research and Technology Network, S.A., 7 Kifissias Ave, 115 23, Athens, Greece.
Zoe CourniaBiomedical Research Foundation, Academy of Athens, 4 Soranou Ephessiou, 115 27, Athens, Greece. zcournia@bioacademy.gr.ORCID 0000-0001-9287-364X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Computer-aided drug design has become an integral part of drug discovery and development in the pharmaceutical and biotechnology industry, and is nowadays extensively used in the lead identification and lead optimization phases. The drug design data resource (D3R) organizes challenges against blinded experimental data to prospectively test computational methodologies as an opportunity for improved methods and algorithms to emerge. We participated in Grand Challenge 2 to predict the crystallographic poses of 36 Farnesoid X Receptor (FXR)-bound ligands and the relative binding affinities for two designated subsets of 18 and 15 FXR-bound ligands. Here, we present our methodology for pose and affinity predictions and its evaluation after the release of the experimental data. For predicting the crystallographic poses, we used docking and physics-based pose prediction methods guided by the binding poses of native ligands. For FXR ligands with known chemotypes in the PDB, we accurately predicted their binding modes, while for those with unknown chemotypes the predictions were more challenging. Our group ranked #1st (based on the median RMSD) out of 46 groups, which submitted complete entries for the binding pose prediction challenge. For the relative binding affinity prediction challenge, we performed free energy perturbation (FEP) calculations coupled with molecular dynamics (MD) simulations. FEP/MD calculations displayed a high success rate in identifying compounds with better or worse binding affinity than the reference (parent) compound. Our studies suggest that when ligands with chemical precedent are available in the literature, binding pose predictions using docking and physics-based methods are reliable; however, predictions are challenging for ligands with completely unknown chemotypes. We also show that FEP/MD calculations hold predictive value and can nowadays be used in a high throughput mode in a lead optimization project provided that crystal structures of sufficiently high quality are available.

Indexed as

Drug DesignThermodynamicsBenzimidazolesBinding SitesComputer-Aided DesignDatabases, ProteinHumansIsoxazolesLigandsMolecular Docking SimulationProtein BindingProtein ConformationReceptor, Farnesoid X-ActivatedReceptors, Cytoplasmic and NuclearSpiro CompoundsSulfonamidesBenzimidazolesIsoxazolesLigandsReceptor, Farnesoid X-ActivatedReceptors, Cytoplasmic and NuclearSpiro CompoundsSulfonamidesD3RDockingDrug design data resourceFarnesoid X receptorFEP+Free energy perturbationFXR

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.