Evidence map›Paper›PMID 34342438›Full record

ArticleJournal of medicinal chemistry2021

Rationally Modified Antimicrobial Peptides from the N-Terminal Domain of Human RNase 3 Show Exceptional Serum Stability.

Daniel Sandín, Javier Valle, Belén Chaves-Arquero, Guillem Prats-Ejarque, María Nieves Larrosa, Juan José González-López, María Ángeles Jiménez, Ester Boix, David Andreu, Marc Torrent

Open access · hybridAbstract read
In one paragraph

Article in Journal of medicinal chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

20 citing papers in PubMed, 32 citations in OpenAlex.

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  12. Functional Insight into hTRIR.Current molecular medicine · 2024
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  19. The future of recombinant host defense peptides.Microbial cell factories · 2022
    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

10 authors at 3 institutions in 1 country.

Daniel SandínDepartment of Biochemistry and Molecular Biology, Universitat Autònoma de Barcelona, Cerdanyola del Vallès 08193, Spain.
Javier ValleDepartment of Experimental and Health Sciences, Universitat Pompeu Fabra, Barcelona Biomedical Research Park, Barcelona 08003, Spain.
Belén Chaves-ArqueroDepartamento de Química-Física Biológica, Instituto de Química Física Rocasolano (IQFR-CSIC), Serrano 119, Madrid 28006, Spain.
Guillem Prats-EjarqueDepartment of Biochemistry and Molecular Biology, Universitat Autònoma de Barcelona, Cerdanyola del Vallès 08193, Spain.
María Nieves LarrosaServei de Microbiologia, Hospital Universitari Vall d'Hebron, Barcelona 08035, Spain.
Juan José González-LópezServei de Microbiologia, Hospital Universitari Vall d'Hebron, Barcelona 08035, Spain.
María Ángeles JiménezDepartamento de Química-Física Biológica, Instituto de Química Física Rocasolano (IQFR-CSIC), Serrano 119, Madrid 28006, Spain.ORCID 0000-0001-6835-5850
Ester BoixDepartment of Biochemistry and Molecular Biology, Universitat Autònoma de Barcelona, Cerdanyola del Vallès 08193, Spain.ORCID 0000-0003-1790-2142
David AndreuDepartment of Experimental and Health Sciences, Universitat Pompeu Fabra, Barcelona Biomedical Research Park, Barcelona 08003, Spain.ORCID 0000-0002-6317-6666
Marc TorrentDepartment of Biochemistry and Molecular Biology, Universitat Autònoma de Barcelona, Cerdanyola del Vallès 08193, Spain.ORCID 0000-0001-6567-3474
Universitat Autònoma de Barcelona · ESInstituto de Química Física Blas Cabrera · ESUniversitat Pompeu Fabra · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Multidrug resistance against conventional antibiotics poses an important threat to human health. In this context, antimicrobial peptides (AMPs) have been extensively studied for their antibacterial activity and promising results have been shown so far. However, AMPs tend to be rather vulnerable to protease degradation, which offsets their therapeutic appeal. Here, we demonstrate how replacing functional residues in the antimicrobial region of human RNase 3-also named eosinophil cationic protein-by non-natural amino acids increases stability in human serum. These changes were also shown to reduce the hemolytic effect of the peptides in general terms, whereas the antimicrobial activity was reasonably preserved. Digestion profiles enabled us to design new peptides with superior stability and lower toxicity that could become relevant candidates to reach clinical stages.

Indexed as

Anti-Bacterial AgentsAntimicrobial Cationic PeptidesDose-Response Relationship, DrugEosinophil Cationic ProteinGram-Negative BacteriaHumansMicrobial Sensitivity TestsMolecular StructureStructure-Activity RelationshipAnti-Bacterial AgentsAntimicrobial Cationic PeptidesEosinophil Cationic ProteinRNASE3 protein, human

Identifiers

PMID34342438
PMCPMC8483441
OpenAlexW3187165927

What OpenQuestion holds

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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.