Evidence map›Paper›PMID 32101691›Full record

ArticleJournal of chemical theory and computation2020

Combining Alchemical Transformation with a Physical Pathway to Accelerate Absolute Binding Free Energy Calculations of Charged Ligands to Enclosed Binding Sites.

Jeffrey Cruz, Lauren Wickstrom, Danzhou Yang, Emilio Gallicchio, Nanjie Deng

Open access · greenAbstract read
In one paragraph

Article in Journal of chemical theory and computation, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.4field-weighted citation impact, top 19% of its field
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

12 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. 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

5 authors at 4 institutions in 1 country.

Jeffrey CruzDepartment of Chemistry and Physical Sciences, Pace University, New York, New York 10038, United States.
Lauren WickstromDepartment of Science, Borough of Manhattan Community College, The City University of New York, New York, New York 10007, United States.ORCID http://orcid.org/0000-0003-4055-3235
Danzhou YangDepartment of Medicinal Chemistry and Molecular Pharmacology, College of Pharmacy, Purdue University, West Lafayette, Indiana 47907, United States.ORCID http://orcid.org/0000-0001-7489-7111
Emilio GallicchioDepartment of Chemistry, Brooklyn College, The City University of New York, Brooklyn, New York 11210, United States.ORCID http://orcid.org/0000-0002-2606-4913
Nanjie DengDepartment of Chemistry and Physical Sciences, Pace University, New York, New York 10038, United States.ORCID http://orcid.org/0000-0001-8805-3526
Pace University · USBorough of Manhattan Community College · USPurdue University West Lafayette · USThe Graduate Center, CUNY · US

Funding

Transgenic Mouse Core Facility Shared Resource (TMCF-SR)P30CA023168 · NCI · PURDUE UNIVERSITY WEST LAFAYETTE · PI Andrea L Kasinski · 1985 to 2026
$43.4M
Targeting MYC promoter G-quadruplex for MYC inhibition by IndenoisoquinolinesR01CA177585 · NCI · UNIVERSITY OF ARIZONA · PI SINTIM, HERMAN O, YANG, DANZHOU · 2014 to 2025
$4.0M
NCI NIH HHS P30 CA023168NCI NIH HHS R01 CA177585
6 · The paper itself

Abstract

We present a new approach to more accurately and efficiently compute the absolute binding free energy for receptor-ligand complexes. Currently, the double decoupling method (DDM) and the potential of mean force method (PMF) are widely used to compute the absolute binding free energy of biomolecular complexes. DDM relies on alchemically decoupling the ligand from its environments, which can be computationally challenging for large ligands and charged ligands because of the large magnitude of the decoupling free energies involved. In contrast, the PMF method uses a physical pathway to directly transfer the ligand from solution to the receptor binding pocket and thus avoids some of the aforementioned problems in DDM. However, the PMF method has its own drawbacks: because of its reliance on a ligand binding/unbinding pathway that is free of steric obstructions from the receptor atoms, the method has difficulty treating ligands with buried atoms. To overcome the limitation in the standard PMF approach and enable buried ligands to be treated, here we develop a new method called AlchemPMF in which steric obstructions along the physical pathway for binding are alchemically removed. We have tested the new approach on two important drug targets involving charged ligands. One is HIV-1 integrase bound to an allosteric inhibitor; the other is the human telomeric DNA G-quadruplex in complex with a natural product protoberberine buried in the binding pocket. For both systems, the new approach leads to more reliable estimates of absolute binding free energies with smaller error bars and closer agreements with experiments compared with those obtained from the existing methods, demonstrating the effectiveness of the new method in overcoming the hysteresis often encountered in PMF binding free energy calculations of such systems. The new approach could also be used to improve the sampling of water equilibration and resolvation of the binding pocket as the ligand is extracted.

Indexed as

G-QuadruplexesBinding SitesEntropyHIV IntegraseLigandsMolecular Dynamics SimulationThermodynamicsHIV IntegraseLigandsp31 integrase protein, Human immunodeficiency virus 1

Identifiers

PMID32101691
PMCPMC7269639
OpenAlexW3007934245

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.