Dokument: Reversing Lanmodulin's Metal‐Binding Sequence in Short Peptides Surprisingly Increases the Lanthanide Affinity

Titel:Reversing Lanmodulin's Metal‐Binding Sequence in Short Peptides Surprisingly Increases the Lanthanide Affinity
URL für Lesezeichen:https://docserv.uni-duesseldorf.de/servlets/DocumentServlet?id=73154
URN (NBN):urn:nbn:de:hbz:061-20260504-111123-9
Kollektion:Publikationen
Sprache:Englisch
Dokumententyp:Wissenschaftliche Texte » Artikel, Aufsatz
Medientyp:Text
Autoren: Gutenthaler-Tietze, Sophie M. [Autor]
Daumann, Lena J. [Autor]
Kretzschmar, Jerome [Autor]
Tsushima, Satoru [Autor]
Steudtner, Robin [Autor]
Drobot, Björn [Autor]
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Dateien vom 04.05.2026 / geändert 04.05.2026
Stichwörter:ITC , EF-hand peptides , NMR , Lanmodulin , Lanthanides , Fluorescence , CD
Beschreibung:Rare earth elements (REEs) are essential for a clean energy future, high tech, and medicine. For these applications the chemically similar elements need to be tediously separated. Recent discoveries that specific lanthanidebinding proteins such as lanmodulin (LanM) exist in nature have prompted the development of bio-inspired separation methods for REEs. Peptides hold great potential for tuning binding sites in various applications as they are easily synthesised, modifiable, and can be immobilised. Here we use the EF-hand binding site sequences of LanM, the naturally
lanthanide-binding EF-hand protein from Methylorubrum extorquens AM1, as a blueprint for peptides with potential
applications in REE recycling. We show with time-resolved laser-induced fluorescence spectroscopy (TRLFS), isothermal titration calorimetry (ITC), and nuclear magnetic resonance (NMR) spectroscopy in combination with molecular dynamics (MD) simulations and circular dichroism (CD) spectroscopy the surprising result that reversing the natural sequence of LanM’s metal-binding loops leads to an increased binding affinity of about one order of magnitude for three out of four natural sequences. Furthermore, we were able to identify structural features responsible for the affinity boost and were able to obtain – only by exchanging one amino acid – a linear uncapped 12-amino-acid peptide with a 150 nM affinity for lanthanides.
Rechtliche Vermerke:Originalveröffentlichung:
Gutenthaler-Tietze, S., Kretzschmar, J., Tsushima, S., Steudtner, R., Drobot, B., & Daumann, L. J. (2025). Reversing Lanmodulin’s Metal‐Binding Sequence in Short Peptides Surprisingly Increases the Lanthanide Affinity. Angewandte Chemie International Edition, 64(46), Article e202510453. https://doi.org/10.1002/anie.202510453
Lizenz:Creative Commons Lizenzvertrag
Dieses Werk ist lizenziert unter einer Creative Commons Namensnennung 4.0 International Lizenz
Fachbereich / Einrichtung:Mathematisch- Naturwissenschaftliche Fakultät
Dokument erstellt am:04.05.2026
Dateien geändert am:04.05.2026
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