Evidence map›Paper›PMID 35059940›Full record

ArticleJournal of computer-aided molecular design2022

Application of the alchemical transfer and potential of mean force methods to the SAMPL8 host-guest blinded challenge.

Solmaz Azimi, Joe Z Wu, Sheenam Khuttan, Tom Kurtzman, Nanjie Deng, Emilio Gallicchio

Abstract read
In one paragraph

Article in Journal of computer-aided molecular design, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Article
  2. Potential distribution theory of alchemical transfer.The Journal of chemical physics · 2025
    Article
  3. Article
  4. Alchemical Enhanced Sampling with Optimized Phase Space Overlap.Journal of chemical theory and computation · 2024
    Article
  5. Article
  6. Review
  7. An overview of the SAMPL8 host-guest binding challenge.Journal of computer-aided molecular design · 2022
    Article
  8. 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

6 authors.

Solmaz AzimiDepartment of Chemistry, Brooklyn College of the City University of New York, Brooklyn NY, USA.
Joe Z WuDepartment of Chemistry, Brooklyn College of the City University of New York, Brooklyn NY, USA.
Sheenam KhuttanDepartment of Chemistry, Brooklyn College of the City University of New York, Brooklyn NY, USA.
Tom KurtzmanPhD Program in Biochemistry, Graduate Center of the City University of New York, New York, NY, USA.
Nanjie DengDepartment of Chemistry and Physical Sciences, Pace University, New York, NY, USA.
Emilio GallicchioDepartment of Chemistry, Brooklyn College of the City University of New York, Brooklyn NY, USA. egallicchio@brooklyn.cuny.edu.ORCID 0000-0002-2606-4913

Funding

Accounting for Water Structure and Thermodynamics in Computer-Aided Drug DesignR01GM100946 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI KURTZMAN, THOMAS PHILIP · 2013 to 2021
$2.7M
Advancing predictive physical modeling through focused development of model systems to drive new modeling innovationsR01GM124270 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI MOBLEY, DAVID LOWELL · 2018 to 2021
$1.5M
Directorate for Mathematical and Physical Sciences 1750511National Science Foundation TG-MCB150001NIGMS NIH HHS R01 GM100946NIGMS NIH HHS R01 GM124270
6 · The paper itself

Abstract

We report the results of our participation in the SAMPL8 GDCC Blind Challenge for host-guest binding affinity predictions. Absolute binding affinity prediction is of central importance to the biophysics of molecular association and pharmaceutical discovery. The blinded SAMPL series have provided an important forum for assessing the reliability of binding free energy methods in an objective way. In this challenge, we employed two binding free energy methods, the newly developed alchemical transfer method (ATM) and the well-established potential of mean force (PMF) physical pathway method, using the same setup and force field model. The calculated binding free energies from the two methods are in excellent quantitative agreement. Importantly, the results from the two methods were also found to agree well with the experimental binding affinities released subsequently, with R values of 0.89 (ATM) and 0.83 (PMF). These results were ranked among the best of the SAMPL8 GDCC challenge and second only to those obtained with the more accurate AMOEBA force field. Interestingly, the two host molecules included in the challenge (TEMOA and TEETOA) displayed distinct binding mechanisms, with TEMOA undergoing a dehydration transition whereas guest binding to TEETOA resulted in the opening of the binding cavity that remains essentially dry during the process. The coupled reorganization and hydration equilibria observed in these systems is a useful prototype for the study of these phenomena often observed in the formation of protein-ligand complexes. Given that the two free energy methods employed here are based on entirely different thermodynamic pathways, the close agreement between the two and their general agreement with the experimental binding free energies are a testament to the high quality and precision achieved by theory and methods. The study provides further validation of the novel ATM binding free energy estimation protocol and paves the way to further extensions of the method to more complex systems.

Indexed as

Molecular Dynamics SimulationProteinsLigandsProtein BindingReproducibility of ResultsThermodynamicsLigandsProteinsBinding free energy estimationComputational alchemyHost-guestPotential of mean forceSAMPL

Identifiers

PMID35059940
PMCPMC8982563

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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.