Evidence map›Paper›PMID 29489903›Full record

ArticlePloS one2018

Design and synthesis of constrained bicyclic molecules as candidate inhibitors of influenza A neuraminidase.

Cinzia Colombo, Črtomir Podlipnik, Leonardo Lo Presti, Masahiro Niikura, Andrew J Bennet, Anna Bernardi

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2018. 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
0.7field-weighted citation impact, top 37% 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, 7 citations in OpenAlex.

  1. Article
  2. Review
  3. Inhibition of sialidase activity as a therapeutic approach.Drug design, development and therapy · 2018
    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

6 authors at 3 institutions in 3 countries.

Cinzia ColomboUniversità degli Studi di Milano, Dipartimento di Chimica, Milano, Italy.ORCID 0000-0002-2917-8801
Črtomir PodlipnikUniversity of Ljubljana, Faculty of Chemistry and Chemical Technology, Ljubljana, Slovenia.
Leonardo Lo PrestiUniversità degli Studi di Milano, Dipartimento di Chimica, Milano, Italy.
Masahiro NiikuraFaculty of Health Sciences, Simon Fraser University, Burnaby, British Columbia, Canada.
Andrew J BennetDepartment of Chemistry, Simon Fraser University, Burnaby, British Columbia, Canada.
Anna BernardiUniversità degli Studi di Milano, Dipartimento di Chimica, Milano, Italy.
Simon Fraser University · CAUniversity of Milan · ITUniversity of Ljubljana · SI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The rise of drug-resistant influenza A virus strains motivates the development of new antiviral drugs, with different structural motifs and substitution. Recently, we explored the use of a bicyclic (bicyclo[3.1.0]hexane) analogue of sialic acid that was designed to mimic the conformation adopted during enzymatic cleavage within the neuraminidase (NA; sialidase) active site. Given that our first series of compounds were at least four orders of magnitude less active than available drugs, we hypothesized that the new carbon skeleton did not elicit the same interactions as the cyclohexene frameworks used previously. Herein, we tried to address this critical point with the aid of molecular modeling and we proposed new structures with different functionalization, such as the introduction of free ammonium and guanidinium groups and ether side chains other than the 3-pentyl side chain, the characteristic side chain in Oseltamivir. A highly simplified synthetic route was developed, starting from the cyclopropanation of cyclopentenone and followed by an aziridination and further functionalization of the five-member ring. This allowed the efficient preparation of a small library of new bicyclic ligands that were characterized by enzyme inhibition assays against influenza A neuraminidases N1, its H274Y mutant, and N2. The results show that none of the new structural variants synthesized, including those containing guanidinium groups rather than free ammonium ions, displayed activity against influenza A neuraminidases at concentrations less than 2 mM. We conclude that the choice and positioning of functional groups on the bicyclo[3.1.0]hexyl system still need to be properly tuned for producing complementary interactions within the catalytic site.

Indexed as

Drug DesignBridged Bicyclo Compounds, HeterocyclicCatalytic DomainChemistry Techniques, SyntheticEnzyme InhibitorsInfluenza A Virus, H5N1 SubtypeInfluenza A Virus, H9N2 SubtypeMolecular Docking SimulationNeuraminidaseViral ProteinsBridged Bicyclo Compounds, HeterocyclicEnzyme InhibitorsNA protein, influenza A virusNeuraminidaseViral Proteins

Identifiers

PMID29489903
PMCPMC5831633
OpenAlexW2790118254

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.