Evidence map›Paper›PMID 31460480›Full record

ArticleACS omega2019

Glycoconjugates Based on Supramolecular Tröger's Base Scaffold: Synthesis, Photophysics, Docking, and BSA Association Study.

Débora Muller Pimentel Aroche, Jaqueline Pinto Vargas, Pablo Andrei Nogara, Fabiano da Silveira Santos, João Batista Teixeira da Rocha, Diogo Seibert Lüdtke, Fabiano Severo Rodembusch

Open access · goldAbstract read
In one paragraph

Article in ACS omega, 2019. 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
1.1field-weighted citation impact, top 26% 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, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. 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

7 authors at 2 institutions in 1 country.

Débora Muller Pimentel ArocheGrupo de Pesquisa em Fotoquímica Orgânica Aplicada, Universidade Federal do Rio Grande do Sul, UFRGS, Instituto de Química, Av. Bento Gonçalves 9500, CEP 91501-970 Porto Alegre, RS, Brazil.
Jaqueline Pinto VargasInstituto de Química, Universidade Federal do Rio Grande do Sul, UFRGS, Av. Bento Gonçalves 9500, 91501-970 Porto Alegre, RS, Brazil.
Pablo Andrei NogaraDepartamento de Bioquímica e Biologia Molecular, Centro de Ciências Naturais e Exatas, Universidade Federal de Santa Maria, UFSM, 97105-900 Santa Maria, RS, Brazil.
Fabiano da Silveira SantosGrupo de Pesquisa em Fotoquímica Orgânica Aplicada, Universidade Federal do Rio Grande do Sul, UFRGS, Instituto de Química, Av. Bento Gonçalves 9500, CEP 91501-970 Porto Alegre, RS, Brazil.
João Batista Teixeira da RochaDepartamento de Bioquímica e Biologia Molecular, Centro de Ciências Naturais e Exatas, Universidade Federal de Santa Maria, UFSM, 97105-900 Santa Maria, RS, Brazil.
Diogo Seibert LüdtkeInstituto de Química, Universidade Federal do Rio Grande do Sul, UFRGS, Av. Bento Gonçalves 9500, 91501-970 Porto Alegre, RS, Brazil.
Fabiano Severo RodembuschGrupo de Pesquisa em Fotoquímica Orgânica Aplicada, Universidade Federal do Rio Grande do Sul, UFRGS, Instituto de Química, Av. Bento Gonçalves 9500, CEP 91501-970 Porto Alegre, RS, Brazil.
Universidade Federal do Rio Grande do Sul · BRUniversidade Federal de Santa Maria · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This study presents new Tröger's bases bearing glycosyl moieties obtained from a copper-catalyzed azide-alkyne cycloaddition reaction. The Tröger's bases present absorption maxima close to 275 nm related to fully spin and symmetry-allowed electronic transitions. The main fluorescence emission located at 350 nm was observed with no influence on the glycosyl moieties. Furthermore, protein detection studies have been performed using bovine serum albumin (BSA) as a model protein, and results have shown a strong interaction between some of the compounds through a static fluorescence suppression mechanism related to the formation of a glycoconjugate-BSA complex favored by the glycosyl subunit. Moreover, docking was also studied for better understanding the suppression mechanism and indicated that the glycosyl and triazole moieties increase the affinity with BSA.

Identifiers

PMID31460480
PMCPMC6705216
OpenAlexW2965097603

What OpenQuestion holds

Textmetadata
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.