Evidence map›Paper›PMID 38398581›Full record

ArticleMolecules (Basel, Switzerland)2024

Machine Learning Methods as a Cost-Effective Alternative to Physics-Based Binding Free Energy Calculations.

Nupur Bansal, Ye Wang, Simone Sciabola

Abstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Review
  2. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Nupur BansalBiotherapeutic and Medicinal Sciences, Biogen, 225 Binney Street, Cambridge, MA 02142, USA.
Ye WangBiotherapeutic and Medicinal Sciences, Biogen, 225 Binney Street, Cambridge, MA 02142, USA.
Simone SciabolaBiotherapeutic and Medicinal Sciences, Biogen, 225 Binney Street, Cambridge, MA 02142, USA.ORCID 0000-0003-1448-3608

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The rank ordering of ligands remains one of the most attractive challenges in drug discovery. While physics-based in silico binding affinity methods dominate the field, they still have problems, which largely revolve around forcefield accuracy and sampling. Recent advances in machine learning have gained traction for protein-ligand binding affinity predictions in early drug discovery programs. In this article, we perform retrospective binding free energy evaluations for 172 compounds from our internal collection spread over four different protein targets and five congeneric ligand series. We compared multiple state-of-the-art free energy methods ranging from physics-based methods with different levels of complexity and conformational sampling to state-of-the-art machine-learning-based methods that were available to us. Overall, we found that physics-based methods behaved particularly well when the ligand perturbations were made in the solvation region, and they did not perform as well when accounting for large conformational changes in protein active sites. On the other end, machine-learning-based methods offer a good cost-effective alternative for binding free energy calculations, but the accuracy of their predictions is highly dependent on the experimental data available for training the model.

Indexed as

Machine LearningProteinsBinding SitesCost-Benefit AnalysisLigandsPhysicsProtein BindingRetrospective StudiesThermodynamicsLigandsProteinsbenchmarkingfree energyligandsreceptorsscreening assays

Identifiers

PMID38398581
PMCPMC10893267

What OpenQuestion holds

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Registered trials

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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.