Evidence map›Paper›PMID 40138324›Full record

ArticleInorganic chemistry2025

Metal-Induced Amide Deprotonation and Binding Typical for Cu(II), Not Possible for Zn(II) and Fe(II).

Silvia Leveraro, Valentyn Dzyhovskyi, Kinga Garstka, Agnieszka Szebesczyk, Fabio Zobi, Denise Bellotti, Kamila Stokowa-Sołtys, Maurizio Remelli, Magdalena Rowińska-Żyrek

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Article in Inorganic chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
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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.

Silvia LeveraroFaculty of Chemistry, University of Wroclaw, ul. F. Joliot-Curie 14, 50-383 Wroclaw, Poland.
Valentyn DzyhovskyiFaculty of Chemistry, University of Wroclaw, ul. F. Joliot-Curie 14, 50-383 Wroclaw, Poland.
Kinga GarstkaFaculty of Chemistry, University of Wroclaw, ul. F. Joliot-Curie 14, 50-383 Wroclaw, Poland.
Agnieszka SzebesczykInstitute of Health Sciences, University of Opole, Katowicka str. 68, 45-060 Opole, Poland.ORCID 0000-0003-3533-1988
Fabio ZobiDepartment of Chemistry, Fribourg University, Chemin Du Musée 9, 1700 Fribourg, Switzerland.ORCID 0000-0002-9077-7184
Denise BellottiDepartment of Chemical, Pharmaceutical and Agricultural Sciences, University of Ferrara, Via Luigi Borsari 46, 44121 Ferrara, Italy.
Kamila Stokowa-SołtysFaculty of Chemistry, University of Wroclaw, ul. F. Joliot-Curie 14, 50-383 Wroclaw, Poland.
Maurizio RemelliDepartment of Chemical, Pharmaceutical and Agricultural Sciences, University of Ferrara, Via Luigi Borsari 46, 44121 Ferrara, Italy.
Magdalena Rowińska-ŻyrekFaculty 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

Amide groups of the peptide backbone are very weak acids. In fact, their deprotonation in water solution is not a phenomenon usually observed in the measuring range of a glass electrode unless the proton is displaced by a metal such as Cu(II) or Ni(II). Other metals are not usually expected to deprotonate and bind to amide nitrogens, although, lately, some controversies have started to arise in the literature, suggesting that Zn(II) and Fe(II) may be capable of doing so. In order to clarify this phenomenon, we chose to study simple metal-peptide systems with Ala-to-Pro mutations, which excluded further amides from binding. A comparison of the metal-binding modes of Ac-AAAHAAA-NH

Identifiers

PMID40138324
PMCPMC11979888

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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.