Evidence map›Paper›PMID 42000821›Full record

ArticleScientific reports2026

Peptide ligands to explore interactions with intrinsically disordered multidomain proteins: the case of SARS-CoV-2 nucleocapsid protein.

A S Tino, M Quagliata, M Schiavina, L Attanasio, B P O Santos, L Pacini, A M Papini, R Pierattelli, I C Felli

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In one paragraph

Article in Scientific reports, 2026. 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
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0citing 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

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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.

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

9 authors.

A S TinoDepartment of Chemistry "Ugo Schiff", University of Florence, Via Della Lastruccia 3-13, 50019, Sesto Fiorentino, Florence, Italy.
M QuagliataDepartment of Chemistry "Ugo Schiff", University of Florence, Via Della Lastruccia 3-13, 50019, Sesto Fiorentino, Florence, Italy.
M SchiavinaDepartment of Chemistry "Ugo Schiff", University of Florence, Via Della Lastruccia 3-13, 50019, Sesto Fiorentino, Florence, Italy.
L AttanasioDepartment of Chemistry "Ugo Schiff", University of Florence, Via Della Lastruccia 3-13, 50019, Sesto Fiorentino, Florence, Italy.
B P O SantosDepartment of Chemistry "Ugo Schiff", University of Florence, Via Della Lastruccia 3-13, 50019, Sesto Fiorentino, Florence, Italy.
L PaciniDepartment of Chemistry "Ugo Schiff", University of Florence, Via Della Lastruccia 3-13, 50019, Sesto Fiorentino, Florence, Italy.
A M PapiniDepartment of Chemistry "Ugo Schiff", University of Florence, Via Della Lastruccia 3-13, 50019, Sesto Fiorentino, Florence, Italy. annamaria.papini@unifi.it.
R PierattelliDepartment of Chemistry "Ugo Schiff", University of Florence, Via Della Lastruccia 3-13, 50019, Sesto Fiorentino, Florence, Italy. roberta.pierattelli@unifi.it.
I C FelliDepartment of Chemistry "Ugo Schiff", University of Florence, Via Della Lastruccia 3-13, 50019, Sesto Fiorentino, Florence, Italy. isabellacaterina.felli@unifi.it.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The SARS-CoV-2 nucleocapsid protein (N), essential for viral RNA packaging, comprises a structured RNA-binding domain, NTD(44-180), flanked by intrinsically disordered regions, IDR1 (1-43) and IDR2 (181-248). This extended, positively charged RNA-binding surface makes it an attractive target for synthetic ligands able to interfere with its function. In this study, peptide ligands were explored as synthetically accessible alternatives for modulating N interactions. After confirming the ability of a reference peptide (P0) in engaging IDRs in the interaction, we shifted our attention to key properties that modulate the interaction with the central domain NTD(44-180). Two new peptides (P1 and P2) were designed with identical amino acid compositions but distinct sequence arrangements. In each one a para-fluorinated phenylalanine residue was incorporated to introduce an aromatic component useful to mimic RNA bases and enable

Indexed as

Coronavirus Nucleocapsid ProteinsIntrinsically Disordered ProteinsNucleocapsid ProteinsPeptidesSARS-CoV-2Binding SitesCircular DichroismHumansLigandsMagnetic Resonance SpectroscopyMolecular Dynamics SimulationPhosphoproteinsProtein BindingProtein DomainsCoronavirus Nucleocapsid ProteinsIntrinsically Disordered ProteinsLigandsnucleocapsid phosphoprotein, SARS-CoV-2Nucleocapsid ProteinsPeptidesPhosphoproteins19F NMR spectroscopyIntrinsically disordered protein regions (IDRs)Molecular dynamics simulationsPeptide-protein interactionsSARS-CoV-2 nucleocapsid proteinSynthetic tailored peptides

Identifiers

PMID42000821
PMCPMC13254127

What Socratic holds

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Registered trials

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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 Socratic graph.