Evidence map›Paper›PMID 41193433›Full record

ArticleJournal of the American Chemical Society2025

Metallo-coiled Coil Stabilization via Chemical Cross-Linking: Implications for Gd(III)-Based MRI Contrast Agents.

Kate A Hadley, Marco Ricci, Marko Hanzevacki, Helena Bernstein, Hiruni S Jayasekera, Aneika C Leney, Adrian J Mulholland, Fabio Carniato, Mauro Botta, Melanie M Britton and 1 more

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 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

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

2 citing papers in PubMed.

  1. Article
  2. Review
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

11 authors.

Kate A HadleySchool of Chemistry, University of Birmingham, Edgbaston B15 2TT, United Kingdom.
Marco RicciDipartimento di Scienze e Innovazione Tecnologica, Università del Piemonte Orientale "A. Avogadro", Alessandria 15121, Italy.
Marko HanzevackiCentre for Computational Chemistry, School of Chemistry, University of Bristol, Bristol BS8 1TS, United Kingdom.ORCID 0000-0002-0834-871X
Helena BernsteinSchool of Biosciences, University of Birmingham, Edgbaston B15 2TT, United Kingdom.
Hiruni S JayasekeraSchool of Biosciences, University of Birmingham, Edgbaston B15 2TT, United Kingdom.
Aneika C LeneySchool of Biosciences, University of Birmingham, Edgbaston B15 2TT, United Kingdom.ORCID 0000-0002-2066-4950
Adrian J MulhollandCentre for Computational Chemistry, School of Chemistry, University of Bristol, Bristol BS8 1TS, United Kingdom.ORCID 0000-0003-1015-4567
Fabio CarniatoDipartimento di Scienze e Innovazione Tecnologica, Università del Piemonte Orientale "A. Avogadro", Alessandria 15121, Italy.ORCID 0000-0002-6268-1687
Mauro BottaDipartimento di Scienze e Innovazione Tecnologica, Università del Piemonte Orientale "A. Avogadro", Alessandria 15121, Italy.ORCID 0000-0003-4192-355X
Melanie M BrittonSchool of Chemistry, University of Birmingham, Edgbaston B15 2TT, United Kingdom.ORCID 0000-0003-3808-1590
Anna F A PeacockSchool of Chemistry, University of Birmingham, Edgbaston B15 2TT, United Kingdom.ORCID 0000-0001-6809-9295

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Coiled coils are a versatile class of protein-inspired metal-binding ligands with well-defined sequence-to-structure relationships and high synthetic accessibility, making them promising tunable ligands for applications spanning biomedical imaging, catalysis, and material science. However, their practical utility is often limited by poor stability, particularly under physiological conditions. Herein, we introduce a covalent interhelical isopeptide cross-linking strategy that significantly enhances the thermal, thermodynamic, kinetic, and proteolytic stability of lanthanide-bound coiled coils designed for use as MRI contrast agents. Biophysical analysis, including CD, native MS, HPLC, and fluorescence assays, reveal that introduction of a single cross-linking layer promotes structural organization, driving the peptide from an unfolded to a well-folded state. Cross-linking leads to a remarkable 2.5 × 10

Indexed as

Contrast MediaCross-Linking ReagentsGadoliniumMagnetic Resonance ImagingPeptidesMolecular Dynamics SimulationProtein StabilityThermodynamicsContrast MediaCross-Linking ReagentsGadoliniumPeptides

Identifiers

PMID41193433
PMCPMC12636026

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.