Cerium binding to proteins: a structural analysis

Abstract

Ce-peptide and Ce-protein adducts can be used to improve stability, solubility, and distribution of Ce ions and Ce complexes within the body and to create artificial metalloenzymes with catalase and superoxide dismutase activities. However, the mechanisms by which Ce is recognized by proteins are not entirely known at the atomic level. Here, a comparative analysis of the few examples of known Ce/protein structures is presented and the results of this analysis are discussed. Ce3+ can replace Ca2+ and Ce4+ can replace Fe3+. Ce ions are mainly located on the side chains of Asp and Glu (in both monodentate and bidentate binding modes) with a large variability in their coordination number. No major global structural rearrangement is apparent in the analyzed examples. However, the dataset used for the analysis is very limited. Thus, this perspective is intended to encourage further research in the field of Ce-protein interaction.

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BibTeX RIS

BibTeX

@article{merlino2026cerium,
  title = {{Cerium binding to proteins: a structural analysis}},
  author = {Antonello Merlino},
  journal = {Frontiers in Chemical Biology},
  year = {2026},
  month = nov,
  doi = {10.3389/fchbi.2026.1981754},
  url = {https://doi.org/10.3389/fchbi.2026.1981754},
  note = {CC BY},
}

RIS

TY  - JOUR
TI  - Cerium binding to proteins: a structural analysis
AU  - Antonello Merlino
PY  - 2026
DA  - 2026/11/05
JO  - Frontiers in Chemical Biology
DO  - 10.3389/fchbi.2026.1981754
UR  - https://doi.org/10.3389/fchbi.2026.1981754
AB  - Ce-peptide and Ce-protein adducts can be used to improve stability, solubility, and distribution of Ce ions and Ce complexes within the body and to create artificial metalloenzymes with catalase and superoxide dismutase activities. However, the mechanisms by which Ce is recognized by proteins are not entirely known at the atomic level. Here, a comparative analysis of the few examples of known Ce/protein structures is presented and the results of this analysis are discussed. Ce3+ can replace Ca2+ and Ce4+ can replace Fe3+. Ce ions are mainly located on the side chains of Asp and Glu (in both monodentate and bidentate binding modes) with a large variability in their coordination number. No major global structural rearrangement is apparent in the analyzed examples. However, the dataset used for the analysis is very limited. Thus, this perspective is intended to encourage further research in the field of Ce-protein interaction.
SN  - 2813-530X
ER  -

Abstract

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