Evidence map›Paper›PMID 35494350›Full record

ArticleRSC advances2021

Development of fructose-1,6-bisphosphate aldolase enzyme peptide mimics as biocatalysts in direct asymmetric aldol reactions.

Thabo Peme, Dean Brady, Wanyama Juma, Maya Makatini

Open access · goldAbstract read
In one paragraph

Article in RSC advances, 2021. 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
0.4field-weighted citation impact, top 42% 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, 5 citations in OpenAlex.

  1. Article
  2. Article
  3. 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 at 1 institution in 1 country.

Thabo PemeMolecular Sciences Institute, School of Chemistry, University of the Witwatersrand Private Bag 3, PO WITS 2050 South Africa maya.makatini@wits.ac.za +27 11 717 6708.
Dean BradyMolecular Sciences Institute, School of Chemistry, University of the Witwatersrand Private Bag 3, PO WITS 2050 South Africa maya.makatini@wits.ac.za +27 11 717 6708.ORCID https://orcid.org/0000-0002-4815-1030
Wanyama JumaMolecular Sciences Institute, School of Chemistry, University of the Witwatersrand Private Bag 3, PO WITS 2050 South Africa maya.makatini@wits.ac.za +27 11 717 6708.
Maya MakatiniMolecular Sciences Institute, School of Chemistry, University of the Witwatersrand Private Bag 3, PO WITS 2050 South Africa maya.makatini@wits.ac.za +27 11 717 6708.ORCID https://orcid.org/0000-0001-7280-0945
University of the Witwatersrand · ZA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This study describes the design and synthesis of mimetic peptides modelled on the catalytic active site of the fructose-1,6-bisphosphate aldolase (FBPA) enzyme. The synthesized peptides consisting of the turn motifs and catalytic site amino acids of FBPA enzyme were evaluated for catalytic activity in direct asymmetric aldol reactions of ketones and aldehydes. The influence of substrate scope, catalyst loading and solvents including water, on the reaction were also investigated. Nuclear magnetic resonance (NMR) and circular dichroism (CD) were used to determine the secondary structure of the peptides to provide an understanding of the structure-activity relationship. The peptides showed catalytic activity and the aldol products were obtained in low yields (up to 44%), but excellent enantioselectivity (up to 93%) and moderate diastereoselectivity (65 : 35).

Identifiers

PMID35494350
PMCPMC9043830
OpenAlexW3213292072

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.