Engineering lanmodulin's selectivity for actinides over lanthanides by controlling solvent coordination and second-sphere interactions.

ABSTRACT: Developing chelators that combine high affinity and selectivity for lanthanides and/or actinides is paramount for numerous industries, including rare earths mining, nuclear waste management, and cancer medicine. In particular, achieving selectivity between actinides and lanthanides is notoriously difficult. The protein lanmodulin (LanM) is one of Nature's most selective chelators for trivalent actinides and lanthanides. However, mechanistic understanding of LanM's affinity and selectivity for f-elements remains limited. In order to decipher, and possibly improve, the features of LanM's metal-binding sites that contribute to this actinide/lanthanide selectivity, we characterized five LanM variants, substituting the aspartate residue at the 9^th position of each metal-binding site

SUBMITTER: Mattocks JA 

PROVIDER: S-EPMC9132084 | biostudies-literature | 2022 May

REPOSITORIES: biostudies-literature