Speaker
Description
Uranium and rare earth mining, the extensive use of mineral fertilizers, nuclear weapons programs, and reprocessing plants have released significant amounts of lanthanides and actinides worldwide. The environmental contamination with f-elements can pose severe health risks, especially if they enter the human food chain. Hence, a deeper understanding of the interaction of f-elements with biochemical motifs is crucial for risk assessment and hazard management.
Studies on metalloproteins like transferrin, calmodulin, and siderocalin have revealed strong interactions with f-elements. Particularly high affinities are found for phosphoproteins like casein or phosvitin, which contain high levels of phosphoserine residues. For a detailed understanding of the binding modes and preferred coordination sites in amino acid/peptide-f-element systems, systematic investigations remain essential.
With this aim, the novel phosphorylation agent (py)2PO2[OTf] (py = pyridine, OTf = triflate) was used to functionalize dipeptides to obtain a library of bio-inspired model compounds. Their interactions with f-elements were subsequently studied. Systems of the unmodified dipeptides as well as the model compounds were investigated in combination with various Ln(III) and uranyl(VI) ions in solution using heteronuclear NMR and fluorescence spectroscopy. The results, including complex stoichiometries and identified coordination sites, are presented.