Dipeptide photodegradation under copper ion influence suggests protective second-shell design in copper-binding proteins.

Xingyi Shi, Huahuan Cai, Wei Tang, Erjun Wei, MingXiao Zhao, Yufen Zhao

Abstract read

In one paragraph

Article in BMC chemistry, 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

0cells of the map it votes in

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

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

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

6 authors.

Xingyi Shi *Qian Xuesen Collaborative Research Center of Astrochemistry and Space Life Sciences, Institute of Drug Discovery Technology, Ningbo University, Ningbo, 315211, China.

Huahuan Cai *Qian Xuesen Collaborative Research Center of Astrochemistry and Space Life Sciences, Institute of Drug Discovery Technology, Ningbo University, Ningbo, 315211, China. caihuahuan@nbu.edu.cn.

Wei TangQian Xuesen Collaborative Research Center of Astrochemistry and Space Life Sciences, Institute of Drug Discovery Technology, Ningbo University, Ningbo, 315211, China.

Erjun WeiQian Xuesen Collaborative Research Center of Astrochemistry and Space Life Sciences, Institute of Drug Discovery Technology, Ningbo University, Ningbo, 315211, China.

MingXiao ZhaoQian Xuesen Collaborative Research Center of Astrochemistry and Space Life Sciences, Institute of Drug Discovery Technology, Ningbo University, Ningbo, 315211, China.

Yufen ZhaoQian Xuesen Collaborative Research Center of Astrochemistry and Space Life Sciences, Institute of Drug Discovery Technology, Ningbo University, Ningbo, 315211, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The evolutionary origin of copper-binding proteins remains a central question in prebiotic chemistry. Modern copper proteins predominantly coordinate copper through histidine and cysteine residues, suggesting that these amino acids were selectively favored during early protein evolution. Here, we propose that ultraviolet (UV) radiation acted as a key selective factor in shaping primordial copper-peptides. Spectroscopic analyses suggest that His

Indexed as

CopperMolecular evolutionOrigin of lifePrebiotic chemistryRedox chemistryUV radiation

Identifiers

PMID42002798

DOI10.1186/s13065-026-01802-4

PMCPMC13224675

What OpenQuestion holds

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LicenceCC BY-NC-ND

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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 OpenQuestion graph.