Evidence map›Paper›PMID 40687693›Full record

ArticleChemical science2025

Europium probe binding to serum albumin and α

Huishan Li, Sally Lok-Wan Ng, Dominic J Black, Wei Han, Robert Pal, David Parker

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 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Review
  2. Article
  3. Dynamic chiral quenching of europium and terbium excited states.Physical chemistry chemical physics : PCCP · 2026
    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

6 authors.

Huishan LiDepartment of Chemistry, Hong Kong Baptist University Kowloon Tong 999077 Hong Kong China davidparker@hkbu.edu.hk.ORCID https://orcid.org/0009-0008-3472-4097
Sally Lok-Wan NgDepartment of Chemistry, Hong Kong Baptist University Kowloon Tong 999077 Hong Kong China davidparker@hkbu.edu.hk.ORCID https://orcid.org/0000-0002-2653-5156
Dominic J BlackDepartment of Chemistry, Durham University South Road Durham DH1 3LE UK.
Wei HanDepartment of Chemistry, Hong Kong Baptist University Kowloon Tong 999077 Hong Kong China davidparker@hkbu.edu.hk.ORCID https://orcid.org/0000-0003-0759-1766
Robert PalDepartment of Chemistry, Durham University South Road Durham DH1 3LE UK.
David ParkerDepartment of Chemistry, Hong Kong Baptist University Kowloon Tong 999077 Hong Kong China davidparker@hkbu.edu.hk.ORCID https://orcid.org/0000-0001-5281-5146

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Combined luminescence studies and stochastic molecular dynamics simulations have revealed for the first time how cooperative hydrophobic binding and reversible metal ion coordination to protein glutamate residues occurs. A combined experimental and theoretical approach has been used to explain the very different free energies of binding observed between three structurally analogous chiral europium(iii) complexes and common variants of serum albumin. In particular, reversible binding of a carboxylate from a glutamate residue was observed; this residue is found in human serum albumin but not the other variants. The binding free energy is exquisitely sensitive to the europium probe structure and charge, and favours complexation of a right handed stereoisomer in the chiral binding pocket. Each process has been visualised by short movies, revealing probe conformational exchange dynamics and the pathway to the protein binding site, on a sub-microsecond timescale.

Identifiers

PMID40687693
PMCPMC12272363

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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.