Non-Covalent and Covalent Binding of New Mixed-Valence Cage-like Polyoxidovanadate Clusters to Lysozyme.
Angew Chem Int Ed Engl
; 63(31): e202406669, 2024 07 29.
Article
em En
| MEDLINE
| ID: mdl-38842919
ABSTRACT
The high-resolution X-ray structures of the model protein lysozyme in the presence of the potential drug [VIVO(acetylacetonato)2] from crystals grown in 1.1â
M NaCl, 0.1â
M sodium acetate at pHâ
4.0 reveal the binding to the protein of different and unexpected mixed-valence cage-like polyoxidovanadates (POVs) [V15O36(OH2)]5-, which non-covalently interacts with the lysozyme surface, [V15O33(OH2)]+ and [V20O51(OH2)]n- (this latter based on an unusual {V18O43} cage) which covalently bind the protein. EPR spectroscopy confirms the partial oxidation of VIV to VV and the formation of mixed-valence species. The results indicate that the interaction with proteins can stabilize the structure of unexpected - both for dimension and architecture - POVs, not observed in aqueous solution.
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1
Base de dados:
MEDLINE
Assunto principal:
Vanadatos
/
Muramidase
Idioma:
En
Ano de publicação:
2024
Tipo de documento:
Article