AI Article Synopsis
- * The study compares the complexation behavior of these metals with Tf using various spectroscopic techniques, revealing that Th and Pu show distinct interactions and limited contamination through colloids.
- * SAXS data suggest that the Tf structures change based on the metal bound, with the order of conformation size showing holoTf as the smallest and Tf complexed with deferoxamine B (DFOB) as the largest.
Article Abstract
Transferrin (Tf) is a glycoprotein that transports iron from the serum to the various organs. Several studies have highlighted that Tf can interact with metals other than Fe(III), including actinides that are chemical and radiological toxics. We propose here to report on the behavior of Th(IV) and Pu(IV) in comparison with Fe(III) upon Tf complexation. We considered UV-Vis and IR data of the M Tf complex (M=Fe, Th, Pu) and combined experimental EXAFS data with MD models. EXAFS data of the first M-O coordination sphere are consistent with the MD model considering 1 synergistic carbonate. Further EXAFS data analysis strongly suggests that contamination by Th/Pu colloids seems to occur upon Tf complexation, but it seems limited. SAXS data have also been recorded for all complexes and also after the addition of Deferoxamine-B (DFOB) in the medium. The Rg values are very close for apoTf, ThTf and PuTf, but slightly larger than for holoTf. Data suggest that the structure of the protein is more ellipsoidal than spherical, with a flattened oblate form. From this data, the following order of conformation size might be considered:holoTf
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http://dx.doi.org/10.1002/chem.202300636 DOI Listing Publication Analysis
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