Evidence map›Paper›PMID 27699553›Full record

ArticleJournal of computer-aided molecular design2017

On the fly estimation of host-guest binding free energies using the movable type method: participation in the SAMPL5 blind challenge.

Nupur Bansal, Zheng Zheng, David S Cerutti, Kenneth M Merz

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Article in Journal of computer-aided molecular design, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Overview of the SAMPL6 host-guest binding affinity prediction challenge.Journal of computer-aided molecular design · 2018
    Article
  6. Article
  7. Overview of the SAMPL5 host-guest challenge: Are we doing better?Journal of computer-aided molecular design · 2017
    Review
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

4 authors.

Nupur BansalDepartment of Chemistry, Michigan State University, 578 South Shaw Lane, East Lansing, MI, 48824-1322, USA.
Zheng ZhengDepartment of Chemistry, Michigan State University, 578 South Shaw Lane, East Lansing, MI, 48824-1322, USA.
David S CeruttiDepartment of Chemistry, Michigan State University, 578 South Shaw Lane, East Lansing, MI, 48824-1322, USA.
Kenneth M MerzDepartment of Chemistry, Michigan State University, 578 South Shaw Lane, East Lansing, MI, 48824-1322, USA. kmerz1@gmail.com.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We review our performance in the SAMPL5 challenge for predicting host-guest binding affinities using the movable type (MT) method. The challenge included three hosts, acyclic Cucurbit[2]uril and two octa-acids with and without methylation at the entrance to their binding cavities. Each host was associated with 6-10 guest molecules. The MT method extrapolates local energy landscapes around particular molecular states and estimates the free energy by Monte Carlo integration over these landscapes. Two blind submissions pairing MT with variants of the KECSA potential function yielded mean unsigned errors of 1.26 and 1.53 kcal/mol for the non-methylated octa-acid, 2.83 and 3.06 kcal/mol for the methylated octa-acid, and 2.77 and 3.36 kcal/mol for Cucurbit[2]uril host. While our results are in reasonable agreement with experiment, we focused on particular cases in which our estimates gave incorrect results, particularly with regard to association between the octa-acids and an adamantane derivative. Working on the hypothesis that differential solvation effects play a role in effecting computed binding affinities for the parent octa-acid and the methylated octa-acid and that the ligands bind inside the pockets (rather than on the surface) we devised a new solvent accessible surface area term to better quantify solvation energy contributions in MT based studies. To further explore this issue a, molecular dynamics potential of mean force (PMF) study indicates that, as found by our docking calculations, the stable binding mode for this ligand is inside (rather than surface bound) the octa-acid cavity whether the entrance is methylated or not. The PMF studies also obtained the correct order for the methylation-induced change in binding affinities and associated the difference, to a large extent to differential solvation effects. Overall, the SAMPL5 challenge yielded in improvements our solvation modeling and also demonstrated the need for thorough validation of input data integrity prior to any computational analysis.

Indexed as

LigandsMolecular Dynamics SimulationBinding SitesCucurbit(n)urilsHydrophobic and Hydrophilic InteractionsMacrocyclic CompoundsMolecular ConformationMolecular StructureProtein BindingProteinsSolventsThermodynamicsCucurbit(n)urilsLigandsMacrocyclic CompoundsProteinsSolventsBinding free energyBlind challengeCucurbiturilMovable typeOcta-acidSAMPL5

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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.