Evidence map›Paper›PMID 32889078›Full record

ArticleBiochimica et biophysica acta. General subjects2020

Biophysical studies of HIV-1 glycoprotein-41 interactions with peptides and small molecules - Effect of lipids and detergents.

Guangyan Zhou, Shidong Chu, Aditya Kohli, Francis C Szoka, Miriam Gochin

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta. General subjects, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.1field-weighted citation impact, top 52% 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

3 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. Article
  3. A targeted covalent small molecule inhibitor of HIV-1 fusion.Chemical communications (Cambridge, England) · 2021
    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 2 institutions in 1 country.

Guangyan ZhouDepartment of Basic Sciences, College of Osteopathic Medicine, Touro University California, Vallejo, CA 94592, United States of America.
Shidong ChuDepartment of Basic Sciences, College of Osteopathic Medicine, Touro University California, Vallejo, CA 94592, United States of America.
Aditya KohliDepartment of Bioengineering and Therapeutic Sciences, UCSF School of Pharmacy, San Francisco, CA 94143, United States of America.
Francis C SzokaDepartment of Bioengineering and Therapeutic Sciences, UCSF School of Pharmacy, San Francisco, CA 94143, United States of America; Department of Pharmaceutical Chemistry, UCSF School of Pharmacy, San Francisco, CA 94143, United States of America.
Miriam GochinDepartment of Basic Sciences, College of Osteopathic Medicine, Touro University California, Vallejo, CA 94592, United States of America; Department of Pharmaceutical Chemistry, UCSF School of Pharmacy, San Francisco, CA 94143, United States of America. Electronic address: miriam.gochin@tu.edu.
University of California, San Francisco · USTouro University California · US

Funding

Structure-based discovery and development of HIV-1 gp41 fusion inhibitorsR01GM087998 · NIGMS · TOURO UNIVERSITY OF CALIFORNIA · PI GOCHIN, MIRIAM · 2010 to 2013
$1.1M
Mechanism of indole compounds as HIV fusion inhibitorsR21AI122847 · NIAID · TOURO UNIVERSITY OF CALIFORNIA · PI GOCHIN, MIRIAM · 2016 to 2017
$393k
NIAID NIH HHS R21 AI122847NIGMS NIH HHS R01 GM087998
6 · The paper itself

Abstract

backgroundThe hydrophobic pocket (HP) of HIV-1 glycoprotein-41 ectodomain is defined by two chains of the N-heptad repeat trimer, within the protein-protein interface that mediates 6HB formation. It is a potential target for inhibitors of viral fusion, but its hydrophobic nature and proximity to membrane in situ has precluded ready analysis of inhibitor interactions.

methodsWe evaluated the sensitivity of

resultsChemical shifts of aromatic fluorines were found to be sensitive to changes in the hydrogen bonding network that occurred when inhibitors transitioned from solvent into the HP or into ordered detergent micelles. Fluorescence intensities and emission maxima of autofluorescent compounds responded to changes in the local environment.

conclusionsGp41 - ligand binding occurred under all conditions, but was diminished in the presence of detergents. NMR and fluorescence studies revealed that dodecylphosphocholine (DPC) was a poor substitute for membrane in this system, while liposomes could mimic the membrane surroundings. GENERAL SIGNIFICANCE: Our findings suggest that development of high potency small molecule binders to the HP may be frustrated by competition between binding to the HP and binding to the bilayer membrane.

Indexed as

CholesterolDetergentsHIV-1HIV Envelope Protein gp41HIV InfectionsHumansLipid BilayersLiposomesModels, MolecularPhospholipidsProtein BindingProtein UnfoldingSmall Molecule LibrariesCholesterolDetergentsHIV Envelope Protein gp41Lipid BilayersLiposomesPhospholipidsSmall Molecule Libraries(19)F NMRDetergentsFluorescenceHIV-1 gp41Hydrophobic pocket interactionsLiposomes

Identifiers

PMID32889078
PMCPMC7540966
OpenAlexW3081887430

What OpenQuestion holds

Textmetadata
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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.