Evaluation of the affinity and selectivity of biomimetic peptides towards uranium by HILIC-ESI-MS/ICP-MS - CEA - Commissariat à l’énergie atomique et aux énergies alternatives Accéder directement au contenu
Poster De Conférence Année : 2023

Evaluation of the affinity and selectivity of biomimetic peptides towards uranium by HILIC-ESI-MS/ICP-MS

Résumé

Understanding and limiting the impact of uranium (U) on man requires the characterization of the interactions of UO₂²⁺, the chemical form of U in vivo, with target biomolecules that are unknown until now1. In this context, biomimetic peptides, designed specifically to mimic the coordination sites of UO₂²⁺ in proteins, are very useful chemical tools to determine the parameters responsible for UO₂²⁺ affinity towards its target proteins and further develop selective decorporating agents2. The aim of this work is to develop a dedicated analytical method to determine in a single step and at physiological pH, the affinity and selectivity of multi-phosphorylated biomimetic peptides for UO₂²⁺. The strategy was based on the simultaneous coupling of hydrophilic interaction liquid chromatography (HILIC) to electrospray ionization mass spectrometry (ESI-MS) and inductively coupled plasma mass spectrometry (ICP-MS)3. Firstly, different sets of UO₂(peptide) complexes were successfully separated using different polar stationary phases, being the first HILIC separations of UO₂²⁺ complexes reported in the literature. A dedicated method had been developed for identifying the separated peptide complexes online by ESI-MS and simultaneously quantifying them by ICP-MS, based on U quantification using external calibration. The effect of several structural parameters of the peptides, such as the number and position of phosphoserine (pSer) residues but also their cyclic/linear structure, on UO₂²⁺ affinity were determined. Results showed that the tetra-phosphorylated cyclic peptide (pS1368) exhibited the highest affinity for UO₂²⁺ in comparison with its linear homologue and with cyclic peptides containing lower number of pSer, while the position of pSer had very little influence on this affinity. Following the same approach, the selectivity of pS1368 was determined in the presence of endogenous cations as potential competitors in biological media. pS1368 was the most selective towards UO₂²⁺, underlying its potential as a promising decorporating agent of this element in vivo
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Dates et versions

cea-04118174 , version 1 (06-06-2023)

Identifiants

  • HAL Id : cea-04118174 , version 1

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Lana Abou Zeid, Albert Pell, Marta Garcia Cortes, Hélène Isnard, Pascale Delangle, et al.. Evaluation of the affinity and selectivity of biomimetic peptides towards uranium by HILIC-ESI-MS/ICP-MS. European Winter Conference on Plasma Spectrochemistry, Jan 2023, Ljubljana, Slovenia. 2023. ⟨cea-04118174⟩
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