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Preorganized Peptide Scaffolds as Mimics of Phosphorylated Proteins Binding Sites with a High Affinity for Uranyl

Matthieu Starck 1 Nathalie Sisommay 1 Fanny A. Laporte 1 Stephane Oros 1 Colette Lebrun 1 Pascale Delangle 1
1 RICC - Reconnaissance Ionique et Chimie de Coordination
SYMMES - SYstèmes Moléculaires et nanoMatériaux pour l’Energie et la Santé : DRF/INAC/SYMMES
Abstract : Cyclic peptides with two phosphoserines and two glutamic acids were developed to mimic high-affinity binding sites for uranyl found in proteins such as osteopontin, which is believed to be a privileged target of this ion in vivo. These peptides adopt a $\beta$-sheet structure that allows the coordination of the latter amino acid side chains in the equatorial plane of the dioxo uranyl cation. Complementary spectroscopic and analytical methods revealed that these cyclic peptides are efficient uranyl chelating peptides with a large contribution from the phosphorylated residues. The conditional affinity constants were measured by following fluorescence tryptophan quenching and are larger than 10$^{10}$ at physiological pH. These compounds are therefore promising models for understanding uranyl chelation by proteins, which is relevant to this actinide ion toxicity.
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https://hal-cea.archives-ouvertes.fr/cea-01745407
Contributor : Jérôme Planès <>
Submitted on : Wednesday, March 28, 2018 - 10:57:29 AM
Last modification on : Friday, July 10, 2020 - 7:58:46 AM

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Matthieu Starck, Nathalie Sisommay, Fanny A. Laporte, Stephane Oros, Colette Lebrun, et al.. Preorganized Peptide Scaffolds as Mimics of Phosphorylated Proteins Binding Sites with a High Affinity for Uranyl. Inorganic Chemistry, American Chemical Society, 2015, 54, pp.11557-11562. ⟨10.1021/acs.inorgchem.5b02249⟩. ⟨cea-01745407⟩

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