Evidence map›Paper›PMID 34948332›Full record

ArticleInternational journal of molecular sciences2021

Conformational Preferences and Antiproliferative Activity of Peptidomimetics Containing Methyl 1'-Aminoferrocene-1-carboxylate and Turn-Forming Homo- and Heterochiral Pro-Ala Motifs.

Monika Kovačević, Mojca Čakić Semenčić, Kristina Radošević, Krešimir Molčanov, Sunčica Roca, Lucija Šimunović, Ivan Kodrin, Lidija Barišić

Abstract 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. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Article
  2. Review
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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.

Monika KovačevićDepartment of Chemistry and Biochemistry, Faculty of Food Technology and Biotechnology, University of Zagreb, 10000 Zagreb, Croatia.ORCID 0000-0002-0756-8243
Mojca Čakić SemenčićDepartment of Chemistry and Biochemistry, Faculty of Food Technology and Biotechnology, University of Zagreb, 10000 Zagreb, Croatia.ORCID 0000-0003-3975-1584
Kristina RadoševićDepartment of Biochemical Engineering, Faculty of Food Technology and Biotechnology, University of Zagreb, 10000 Zagreb, Croatia.ORCID 0000-0001-5156-1893
Krešimir MolčanovDivision of Physical Chemistry, Ruđer Bošković Institute, 10000 Zagreb, Croatia.ORCID 0000-0002-4328-3181
Sunčica RocaNMR Centre, Ruđer Bošković Institute, 10000 Zagreb, Croatia.ORCID 0000-0001-9562-6820
Lucija ŠimunovićDepartment of Chemistry and Biochemistry, Faculty of Food Technology and Biotechnology, University of Zagreb, 10000 Zagreb, Croatia.
Ivan KodrinDepartment of Organic Chemistry, Faculty of Science, University of Zagreb, 10000 Zagreb, Croatia.ORCID 0000-0001-6353-3187
Lidija BarišićDepartment of Chemistry and Biochemistry, Faculty of Food Technology and Biotechnology, University of Zagreb, 10000 Zagreb, Croatia.ORCID 0000-0003-3628-7501

Funding

Croatian Science Foundation IP-2014-09-7899 and IP-2020-02-9162
6 · The paper itself

Abstract

The concept of peptidomimetics is based on structural modifications of natural peptides that aim not only to mimic their 3D shape and biological function, but also to reduce their limitations. The peptidomimetic approach is used in medicinal chemistry to develop drug-like compounds that are more active and selective than natural peptides and have fewer side effects. One of the synthetic strategies for obtaining peptidomimetics involves mimicking peptide α-helices, β-sheets or turns. Turns are usually located on the protein surface where they interact with various receptors and are therefore involved in numerous biological events. Among the various synthetic tools for turn mimetic design reported so far, our group uses an approach based on the insertion of different ferrocene templates into the peptide backbone that both induce turn formation and reduce conformational flexibility. Here, we conjugated methyl 1'-aminoferrocene-carboxylate with homo- and heterochiral Pro-Ala dipeptides to investigate the turn formation potential and antiproliferative properties of the resulting peptidomimetics

Indexed as

Carboxylic AcidsCell Line, TumorCell ProliferationCell SurvivalCrystallography, X-RayDipeptidesFerrous CompoundsHeLa CellsHumansMCF-7 CellsPeptidesPeptidomimeticsProtein Structure, SecondaryStereoisomerism1'-aminoferrocene-1-carboxylic acidCarboxylic AcidsDipeptidesFerrous CompoundsPeptidesPeptidomimeticsantiproliferative activitychiralityconformational analysisdensity functional theory (DFT)ferrocenehydrogen bondspeptidomimeticX-ray

Identifiers

PMID34948332
PMCPMC8705031

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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.