Evidence map›Paper›PMID 34065004›Full record

ArticleInternational journal of molecular sciences2021

Phosphinotripeptidic Inhibitors of Leucylaminopeptidases.

Michał Jewgiński, Kinga Haremza, Jesús M de Los Santos, Zouhair Es Sbai, Bartosz Oszywa, Małgorzata Pawełczak, Francisco Palacios, Rafał Latajka

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.2field-weighted citation impact, top 48% 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

0 citing papers in PubMed, 4 citations in OpenAlex.

No citing paper in PubMed yet.

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

8 authors at 3 institutions in 2 countries.

Michał JewgińskiDepartment of Bioorganic Chemistry, Wrocław University of Science and Technology, Wybrzeże Wyspiańskiego 27, 50-370 Wrocław, Poland.ORCID 0000-0003-4931-5452
Kinga HaremzaDepartment of Bioorganic Chemistry, Wrocław University of Science and Technology, Wybrzeże Wyspiańskiego 27, 50-370 Wrocław, Poland.
Jesús M de Los SantosDepartment of Organic Chemistry I, Faculty of Pharmacy, Lascaray Research Center, University of the Basque Country (UPV/EHU), Paseo de la Universidad, 7, 01006 Vitoria, Spain.ORCID 0000-0003-1315-4263
Zouhair Es SbaiDepartment of Organic Chemistry I, Faculty of Pharmacy, Lascaray Research Center, University of the Basque Country (UPV/EHU), Paseo de la Universidad, 7, 01006 Vitoria, Spain.
Bartosz OszywaInstitute of Chemistry, University of Opole, Oleska 48, 45-052 Opole, Poland.
Małgorzata PawełczakInstitute of Chemistry, University of Opole, Oleska 48, 45-052 Opole, Poland.ORCID 0000-0002-3382-9697
Francisco PalaciosDepartment of Organic Chemistry I, Faculty of Pharmacy, Lascaray Research Center, University of the Basque Country (UPV/EHU), Paseo de la Universidad, 7, 01006 Vitoria, Spain.ORCID 0000-0001-6365-0324
Rafał LatajkaDepartment of Bioorganic Chemistry, Wrocław University of Science and Technology, Wybrzeże Wyspiańskiego 27, 50-370 Wrocław, Poland.ORCID 0000-0003-2943-2838
University of the Basque Country · ESWrocław University of Science and Technology · PLUniversity of Opole · PL

Funding

Gobierno Vasco (GV) IT 992-16Ministerio de Ciencia, Innovación y Universidades (MCIU), Agencia Estatal de Investigación (AEI) y Fondo Europeo de Desarrollo Regional (FEDER) RTI2018-101818-B-I00, UEWroclaw Research Center EIT+ under the project "Biotechnologies and advanced medical technologies - BioMed" POIG 01.01.02-02-003/08-00
6 · The paper itself

Abstract

Phosphinate pseudopeptide are analogs of peptides containing phosphinate moiety in a place of the amide bond. Due to this, the organophosphorus fragment resembles the tetrahedral transition state of the amide bond hydrolysis. Additionally, it is also capable of coordinating metal ions, for example, zinc or magnesium ions. These two properties of phosphinate pseudopeptides make them an ideal candidate for metal-related protease inhibitors. This research investigates the influence of additional residue in the P2 position on the inhibitory properties of phosphinopeptides. The synthetic strategy is proposed, based on retrosynthetic analysis. The N-C-P bond formation in the desired compounds is conveniently available from the three-component condensation of appropriate amino components, aldehydes, and hypophosphorous acid. One of the crucial synthetic steps is the careful selection of the protecting groups for all the functionals. Determination of the inhibitor activity of the obtained compounds has been done using UV-Vis spectroscopy and standard substrate

Indexed as

AnimalsEnzyme InhibitorsLeucyl AminopeptidaseModels, MolecularPeptide FragmentsPhosphinesProtein ConformationSwineEnzyme InhibitorsLeucyl AminopeptidasePeptide FragmentsphosphinePhosphinesbarley aminopeptidase inhibitorLAP inhibitorsligand-enzyme interactionmolecular modelingorganophosphorus compoundphosphinate pseudopeptide

Identifiers

PMID34065004
PMCPMC8151835
OpenAlexW3160206103

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.