Evidence map›Paper›PMID 36091973›Full record

ArticleInorganic chemistry frontiers2022

Lanmodulin peptides - unravelling the binding of the EF-Hand loop sequences stripped from the structural corset.

Sophie M Gutenthaler, Satoru Tsushima, Robin Steudtner, Manuel Gailer, Anja Hoffmann-Röder, Björn Drobot, Lena J Daumann

Open access · hybridAbstract read
In one paragraph

Article in Inorganic chemistry frontiers, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.8field-weighted citation impact, top 5% of its field
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

25 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Machine learning-based development of Gadolinium binding peptides.bioRxiv : the preprint server for biology · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. A novel protein for bioremediation of gadolinium waste.Protein science : a publication of the Protein Society · 2025
    Article
  13. Review
  14. Article
  15. Article
  16. Lanthanide binding peptide surfactants at air-aqueous interfaces for interfacial separation of rare earth elements.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  17. Article
  18. Review
  19. Review
  20. 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

7 authors at 3 institutions in 2 countries.

Sophie M GutenthalerDepartment of Chemistry Ludwig-Maximilians-University Munich Butenandtstraße 5-13 81377 München Germany lena.daumann@lmu.de.ORCID https://orcid.org/0000-0002-8412-3328
Satoru TsushimaInstitute of Resource Ecology Helmholtz-Zentrum Dresden-Rossendorf e.V. Bautzner Landstraße 400 01328 Dresden Germany b.drobot@hzdr.de.ORCID https://orcid.org/0000-0002-4520-6147
Robin SteudtnerInstitute of Resource Ecology Helmholtz-Zentrum Dresden-Rossendorf e.V. Bautzner Landstraße 400 01328 Dresden Germany b.drobot@hzdr.de.ORCID https://orcid.org/0000-0002-3103-9587
Manuel GailerDepartment of Chemistry Ludwig-Maximilians-University Munich Butenandtstraße 5-13 81377 München Germany lena.daumann@lmu.de.ORCID https://orcid.org/0000-0003-3052-0472
Anja Hoffmann-RöderDepartment of Chemistry Ludwig-Maximilians-University Munich Butenandtstraße 5-13 81377 München Germany lena.daumann@lmu.de.ORCID https://orcid.org/0000-0002-8352-8323
Björn DrobotInstitute of Resource Ecology Helmholtz-Zentrum Dresden-Rossendorf e.V. Bautzner Landstraße 400 01328 Dresden Germany b.drobot@hzdr.de.ORCID https://orcid.org/0000-0003-1245-0466
Lena J DaumannDepartment of Chemistry Ludwig-Maximilians-University Munich Butenandtstraße 5-13 81377 München Germany lena.daumann@lmu.de.ORCID https://orcid.org/0000-0003-2197-136X
Ludwig-Maximilians-Universität München · DEHelmholtz-Zentrum Dresden-Rossendorf · DETokyo Institute of Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lanmodulin (LanM), a naturally lanthanide (Ln)-binding protein with a remarkable selectivity for Lns over Ca(ii) and affinities in the picomolar range, is an attractive target to address challenges in Ln separation. Why LanM has such a high selectivity is currently not entirely understood; both specific amino acid sequences of the EF-Hand loops and cooperativity effects have been suggested. Here, we removed the effect of cooperativity and synthesised all four 12-amino acid EF-Hand loop peptides, and investigated their affinity for two Lns (Eu(iii) and Tb(iii)), the actinide Cm(iii) and Ca(ii). Using isothermal titration calorimetry and time-resolved laser fluorescence spectroscopy (TRLFS) combined with parallel factor analysis, we show that the four short peptides behave very similarly, having affinities in the micromolar range for Eu(iii) and Tb(iii). Ca(ii) was shown not to bind to the peptides, which was verified with circular dichroism spectroscopy. This technique also revealed an increase in structural organisation upon Eu(iii) addition, which was supported by molecular dynamics simulations. Lastly, we put Eu(iii) and Cm(iii) in direct competition using TRLFS. Remarkably, a slightly higher affinity for Cm(iii) was found. Our results demonstrate that the picomolar affinities in LanM are largely an effect of pre-structuring and therefore a reduction of flexibility in combination with cooperative effects, and that all EF-Hand loops possess similar affinities when detached from the protein backbone, albeit still retaining the high selectivity for lanthanides and actinides over calcium.

Identifiers

PMID36091973
PMCPMC9362731
OpenAlexW4285151684

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

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.