Evidence map›Paper›PMID 38946498›Full record

ArticleInorganic chemistry2024

Zn(II) and Cu(II) Coordination Enhances the Antimicrobial Activity of Piscidin 3, but Not That of Piscidins 1 and 2.

Miller Adriana, Mikołajczyk Aleksandra, Bellotti Denise, Garstka Kinga, Wątły Joanna, Hecel Aleksandra, Wieczorek Robert, Matera-Witkiewicz Agnieszka, Rowińska-Żyrek Magdalena

Abstract read
In one paragraph

Article in Inorganic chemistry, 2024. 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.

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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

9 authors.

Miller AdrianaFaculty of Chemistry, University of Wroclaw, ul. F. Joliot-Curie 14, 50-383 Wroclaw, Poland.
Mikołajczyk AleksandraScreening of Biological Activity Assays and Collection of Biological Material Laboratory, Wroclaw Medical University Biobank, Faculty of Pharmacy, Wroclaw Medical University, ul. Borowska 211a, 50-556 Wroclaw, Poland.
Bellotti DeniseDepartment of Chemical, Pharmaceutical and Agricultural Sciences, University of Ferrara, Via Luigi Borsari 46, 44121 Ferrara, Italy.
Garstka KingaFaculty of Chemistry, University of Wroclaw, ul. F. Joliot-Curie 14, 50-383 Wroclaw, Poland.
Wątły JoannaFaculty of Chemistry, University of Wroclaw, ul. F. Joliot-Curie 14, 50-383 Wroclaw, Poland.ORCID 0000-0003-3770-5189
Hecel AleksandraFaculty of Chemistry, University of Wroclaw, ul. F. Joliot-Curie 14, 50-383 Wroclaw, Poland.ORCID 0000-0002-4314-9599
Wieczorek RobertFaculty of Chemistry, University of Wroclaw, ul. F. Joliot-Curie 14, 50-383 Wroclaw, Poland.
Matera-Witkiewicz AgnieszkaScreening of Biological Activity Assays and Collection of Biological Material Laboratory, Wroclaw Medical University Biobank, Faculty of Pharmacy, Wroclaw Medical University, ul. Borowska 211a, 50-556 Wroclaw, Poland.
Rowińska-Żyrek MagdalenaFaculty of Chemistry, University of Wroclaw, ul. F. Joliot-Curie 14, 50-383 Wroclaw, Poland.ORCID 0000-0002-0425-1128

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Piscidins, antimicrobial peptides isolated from fish, are potent against a variety of human pathogens; they show minimum inhibitory concentration values comparable to those of commercially used antimicrobials. Piscidins 1 and 2 are generally more effective than piscidin 3 when applied alone; the contrary is observed for their metal complexes: Zn(II) and Cu(II) coordination does not enhance the efficacy of piscidins 1 and 2, while a moderate enhancement is observed for piscidin 3. All three piscidins bind Cu(II) in a so-called albumin-like binding mode, while for Zn(II) complexes, two coordination modes are observed: piscidins 1 and 2 bind Zn(II) by imidazole nitrogens from His4, His11, and His17 side chains; piscidin 3 coordinates Zn(II) by His3, His4, and His11 imidazole nitrogens and additionally supports the interaction, formed by carbonyl oxygen from His4. Most likely, the high antimicrobial activity of piscidin complexes is due to neither the stability of their complexes nor the change in their secondary structure. Copper(II) complexes with piscidins 1 and 2 can form hydroxyl radicals, which could be responsible for the antimicrobial membrane damaging activity of these complexes. Clearly, a different mechanism (most likely an intercellular targeted one) is observed for piscidin 3 metal complexes; in most cases, the coordination of Cu(II) and Zn(II) enhances the antimicrobial potency of piscidin 3, showing that not only piscidin 3 alone but also its metal complexes have a different mode of action than piscidins 1 and 2.

Indexed as

Anti-Bacterial AgentsAntimicrobial Cationic PeptidesCoordination ComplexesCopperMicrobial Sensitivity TestsZincAnimalsFish ProteinsAnti-Bacterial AgentsAntimicrobial Cationic PeptidesCoordination ComplexesCopperFish Proteinsmoronecidin protein, Morone saxatilisZinc

Identifiers

PMID38946498
PMCPMC11256756

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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.