Revisiting binding of plutonium to transferrin by CE-ICP-MS

Sauge‐Merle, Sandrine; Lemaire, David; Evans, Robert W.; Berthomieu, Catherine; Aupiais, Jean

doi:10.1039/c6dt04336d

Cited by 15 publications

(18 citation statements)

References 34 publications

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“…Furthermore, the long‐term exposure of actinides to the human body is of major interest. CE‐ICP‐MS has been used for investigation of actinide‐protein binding properties .…”

Section: Analytical Applicationsmentioning

confidence: 99%

Recent advances in capillary electrophoresis‐mass spectrometry: Instrumentation, methodology and applications

et al. 2018

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Capillary electrophoresis (CE) offers fast and high‐resolution separation of charged analytes from small injection volumes. Coupled to mass spectrometry (MS), it represents a powerful analytical technique providing (exact) mass information and enables molecular characterization based on fragmentation. Although hyphenation of CE and MS is not straightforward, much emphasis has been placed on enabling efficient ionization and user‐friendly coupling. Though several interfaces are now commercially available, research on more efficient and robust interfacing with nano‐electrospray ionization (ESI), matrix‐assisted laser desorption/ionization (MALDI) and inductively coupled plasma mass spectrometry (ICP) continues with considerable results. At the same time, CE‐MS has been used in many fields, predominantly for the analysis of proteins, peptides and metabolites. This review belongs to a series of regularly published articles, summarizing 248 articles covering the time between June 2016 and May 2018. Latest developments on hyphenation of CE with MS as well as instrumental developments such as two‐dimensional separation systems with MS detection are mentioned. Furthermore, applications of various CE‐modes including capillary zone electrophoresis (CZE), nonaqueous capillary electrophoresis (NACE), capillary gel electrophoresis (CGE) and capillary isoelectric focusing (CIEF) coupled to MS in biological, pharmaceutical and environmental research are summarized.

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“…Furthermore, the long‐term exposure of actinides to the human body is of major interest. CE‐ICP‐MS has been used for investigation of actinide‐protein binding properties .…”

Section: Analytical Applicationsmentioning

confidence: 99%

Recent advances in capillary electrophoresis‐mass spectrometry: Instrumentation, methodology and applications

et al. 2018

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“…Recently, Sauge-Merle et al . 13 used capillary electrophoresis coupled with an inductively coupled plasma mass spectrometer (CE-ICPMS) to investigate the binding constant of human Tf for Pu IV , and found log 10 K* 1 = 25.0 at pH 6, 0.1 M NaCl, and 25 °C. Therefore, even though another uptake pathway not involving the Tf receptor-mediated system has been suggested as a source of intracellular Pu, this system can partially explain the accumulation of Pu IV in the liver 14–16 .…”

Section: Introductionmentioning

confidence: 99%

Fetuin exhibits a strong affinity for plutonium and may facilitate its accumulation in the skeleton

Vidaud

Miccoli²,

Brulfert

et al. 2019

Sci Rep

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After entering the blood, plutonium accumulates mainly in the liver and the bones. The mechanisms leading to its accumulation in bone are, however, completely unknown. We already know that another uptake pathway not involving the transferrin-mediated pathways is suspected to intervene in the case of the liver. Fetuin, a protein playing an important role in bone metabolism, is proposed as a potential transporter of Pu from serum to bone. For the first time, the binding constants of these two proteins (transferrin and fetuin) with tetravalent plutonium at physiological pH (pH 7.0) were determined by using capillary electrophoresis (CE) coupled with inductively coupled plasma mass spectrometry (ICP-MS). Their very close values (log10 KPuTf = 26.44 ± 0.28 and log10 KPuFet = 26.20 ± 0.24, respectively) suggest that transferrin and fetuin could compete to chelate plutonium, either in the blood or directly at bone surfaces in the case of Pu deposits. We performed competition reaction studies demonstrating that the relative distribution of Pu-protein complexes is fully explained by thermodynamics. Furthermore, considering the average concentrations of transferrin and fetuin in the blood, our calculation is consistent with the bio-distribution of Pu observed in humans.

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“…However, the Fe-OTyr188 bond is very strong (∼2.1 Å) in the embedded model which lead to very large HFCC (−14.5 MHz) due to stronger Fe-OTyr188 interaction. Conversely, 17 O HFCC of Asp65 in the embedded model is smaller (−14.0 MHz) as compared to the isolated model (−17.3 MHz). These variations are due to stronger Fe-OAsp bond in the isolated model (∼1.9 Å), whereas in the embedded model this distance is slightly longer (∼2.1 Å).…”

Section: Mb and Epr Spin Hamiltonian Parametersmentioning

confidence: 80%

“…Our computed MB parameters are in line with the experimental data only when OTyr188 is bound to Fe. Further, 17 O HFCC of Tyr188 is very large (−14.5 MHz) when bound to Fe as compared to unbound state (−1.5 MHz) which can be measured with paramagnetic NMR experiments.…”

Section: Discussionmentioning

confidence: 98%

“…For both isolated and embedded models, the 17 O HFCC of carbonates (∼ −7 to 8 MHz), Tyr95 (∼ −15 MHz) and 14 N of His249 (∼ −8.2 MHz) are very similar. However, the computed HFCC of 17 O Tyr188 in the isolated model is very small (−1.5 MHz) due to very long Fe-OTyr188 (more than 3 Å) thus the oxygen interaction with high spin Fe(III) is rather weak. However, the Fe-OTyr188 bond is very strong (∼2.1 Å) in the embedded model which lead to very large HFCC (−14.5 MHz) due to stronger Fe-OTyr188 interaction.…”

Section: Mb and Epr Spin Hamiltonian Parametersmentioning

confidence: 97%

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Quantum chemical studies of structures and spin Hamiltonian parameters of iron transferrin using isolated and embedded clusters models

Mishra

Sundararajan

2019

J Chem Sci

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Density functional theory (DFT) based calculations using large cluster models are used to elucidate the ground state electronic structure of iron bound transferrin. Explicit incorporation of second coordination amino acid residues and crystallographic water molecules anchors the active site. Our calculations clearly suggest that tyrosine amino acid (Tyr188) residue is bound to iron when the structures are optimized within the continuum solvation model. However, in the gas phase optimized structure, we note that Tyr188 is unbound to Fe (by more than 3 Å). The Mössbauer isomer shift (δ) and quadrupolar splitting (E q) of iron transferrin are in line with the experimental data only when Tyr188 is bound to Fe(III). Further, the computed oxygen hyperfine coupling constant value is very large (−14.5 MHz) when bound to iron which can be verified through 17 O NMR experiments. We propose that Tyr188 is strongly bound to Fe(III) at physiological pH, which needs to be protonated (acidic pH) to weaken this bond, thus the metal release pathway can be possible only in acidic conditions.

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Revisiting binding of plutonium to transferrin by CE-ICP-MS

Cited by 15 publications

References 34 publications

Recent advances in capillary electrophoresis‐mass spectrometry: Instrumentation, methodology and applications

Recent advances in capillary electrophoresis‐mass spectrometry: Instrumentation, methodology and applications

Fetuin exhibits a strong affinity for plutonium and may facilitate its accumulation in the skeleton

Quantum chemical studies of structures and spin Hamiltonian parameters of iron transferrin using isolated and embedded clusters models

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