Selective removal of copper from complex biological media with an agarose-immobilized high-affinity PSP ligand.
J Biol Inorg Chem
; 29(5): 531-540, 2024 Aug.
Article
em En
| MEDLINE
| ID: mdl-39066798
ABSTRACT
The elucidation of metal-dependent biological processes requires selective reagents for manipulating metal ion levels within biological solutions such as growth media or cell lysates. To this end, we immobilized a phosphine sulfide-stabilized phosphine (PSP) ligand on agarose to create a resin for the selective removal of copper from chemically complex biological media through simple filtration or centrifugation. Comprised of a conformationally preorganized phenylene-bridged backbone, the PSP-ligand binds Cu(I) with a 11 stoichiometry and exhibits a pH-independent Cu(I) dissociation constant in the low zeptomolar range. Neither Zn(II), Fe(II), nor Mn(II) interact with the ligand at millimolar concentrations, thus offering a much-improved selectivity towards copper over other commonly employed solid-supported chelators such as Chelex 100. As revealed by X-ray fluorescence elemental analysis, the immobilized chelator effectively removes copper from cell culture growth media and cell lysate isolated from mouse fibroblasts. In addition to preparing copper-depleted media or cell lysates for biological studies, PSP-immobilized ligands might prove equally useful for applications in radiochemistry, materials science, and environmental science.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fosfinas
/
Sefarose
/
Quelantes
/
Cobre
Limite:
Animals
Idioma:
En
Revista:
J Biol Inorg Chem
Assunto da revista:
BIOQUIMICA
Ano de publicação:
2024
Tipo de documento:
Article
País de afiliação:
Estados Unidos
País de publicação:
Alemanha