Evidence map›Paper›PMID 39886434›Full record

ArticleChemical science2025

Cu(ii) binding to an antimicrobial shrimp peptide - a small step for structural chemistry, a big leap for medicinal applications.

Adriana Miller, Agnieszka Matera-Witkiewicz, Aleksandra Mikołajczyk-Tarnawa, Arian Kola, Magdalena Wiloch, Martin Jonsson-Niedziolka, Robert Wieczorek, Joanna Wątły, Daniela Valensin, Magdalena Rowińska-Żyrek

Abstract read
In one paragraph

Article in Chemical science, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
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.

Adriana MillerFaculty of Chemistry, University of Wrocław ul. F. Joliot-Curie 14 50-383 Wrocław Poland magdalena.rowinska-zyrek@uwr.edu.pl.ORCID https://orcid.org/0000-0002-9722-2755
Agnieszka Matera-WitkiewiczScreening of Biological Activity Assays and Collection of Biological Material Laboratory, Wrocław Medical University Biobank, Faculty of Pharmacy, Wrocław Medical University ul. Borowska 211A 50-556 Wrocław Poland.ORCID https://orcid.org/0000-0002-1064-1237
Aleksandra Mikołajczyk-TarnawaScreening of Biological Activity Assays and Collection of Biological Material Laboratory, Wrocław Medical University Biobank, Faculty of Pharmacy, Wrocław Medical University ul. Borowska 211A 50-556 Wrocław Poland.
Arian KolaDepartment of Biotechnology, Chemistry and Pharmacy, University of Siena Via Aldo Moro 2 53100 Siena Italy.ORCID https://orcid.org/0000-0001-9803-9015
Magdalena WilochInstitute of Physical Chemistry, Polish Academy of Sciences ul. Marcina Kasprzaka 44/52 01-224 Warszawa Poland.ORCID https://orcid.org/0000-0001-8331-8572
Martin Jonsson-NiedziolkaInstitute of Physical Chemistry, Polish Academy of Sciences ul. Marcina Kasprzaka 44/52 01-224 Warszawa Poland.ORCID https://orcid.org/0000-0001-5642-5946
Robert WieczorekFaculty of Chemistry, University of Wrocław ul. F. Joliot-Curie 14 50-383 Wrocław Poland magdalena.rowinska-zyrek@uwr.edu.pl.
Joanna WątłyFaculty of Chemistry, University of Wrocław ul. F. Joliot-Curie 14 50-383 Wrocław Poland magdalena.rowinska-zyrek@uwr.edu.pl.ORCID https://orcid.org/0000-0003-3770-5189
Daniela ValensinDepartment of Biotechnology, Chemistry and Pharmacy, University of Siena Via Aldo Moro 2 53100 Siena Italy.ORCID https://orcid.org/0000-0003-4187-3919
Magdalena Rowińska-ŻyrekFaculty of Chemistry, University of Wrocław ul. F. Joliot-Curie 14 50-383 Wrocław Poland magdalena.rowinska-zyrek@uwr.edu.pl.ORCID https://orcid.org/0000-0002-0425-1128

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PvHCt, a 23-amino acid long, histidine-rich peptide derived from shrimp, becomes strongly antimicrobial upon Cu(ii) ion binding. We describe Zn(ii) and Cu(ii) complexes of this peptide, aiming to understand how metal binding and structure correlates to biological activity. Using NMR, UV-vis, CD and FTIR spectroscopies, along with cyclic voltammetry, potentiometry, and DFT calculations, we demonstrate that Cu(ii) binds to the central and C-terminal regions of the peptide, inducing significant structural changes. These include a pronounced bend in the peptide backbone, increased α-helical content, and the production of reactive oxygen species, all of which contribute to the remarkable antimicrobial potency of PvHCt. In contrast, Zn(ii) binds to the C-terminal region with minimal impact on the peptide's overall structure, failing to enhance its antimicrobial activity.

Identifiers

PMID39886434
PMCPMC11775653

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.