High-resolution crystal structures of lysozyme in the presence of the potential drug (VO)-O-IV-(acetylacetonato)2 under two different experimental conditions have been solved. The crystallographic study reveals the loss of the ligands, the oxidation of V-IV to V-V and the subsequent formation of adducts of the protein with two different polyoxidovanadates: [V4O12](4-), which interacts with lysozyme non-covalently, and the unprecedented [V20O54(NO3)](n-), which is covalenty bound to the side chain of an aspartate residue of symmetry related molecules.
Stabilization and Binding of [V4O12]4− and Unprecedented [V20O54(NO3)]n− to Lysozyme upon Loss of Ligands and Oxidation of the Potential Drug VIVO(acetylacetonato)2 / Ferraro, Giarita; Tito, Gabriella; Sciortino, Giuseppe; Garribba, Eugenio; Merlino, Antonello. - In: ANGEWANDTE CHEMIE. INTERNATIONAL EDITION. - ISSN 1433-7851. - 62:50(2023), p. e202310655. [10.1002/anie.202310655]
Stabilization and Binding of [V4O12]4− and Unprecedented [V20O54(NO3)]n− to Lysozyme upon Loss of Ligands and Oxidation of the Potential Drug VIVO(acetylacetonato)2
Sciortino, Giuseppe;Garribba, Eugenio
;Merlino, Antonello
2023-01-01
Abstract
High-resolution crystal structures of lysozyme in the presence of the potential drug (VO)-O-IV-(acetylacetonato)2 under two different experimental conditions have been solved. The crystallographic study reveals the loss of the ligands, the oxidation of V-IV to V-V and the subsequent formation of adducts of the protein with two different polyoxidovanadates: [V4O12](4-), which interacts with lysozyme non-covalently, and the unprecedented [V20O54(NO3)](n-), which is covalenty bound to the side chain of an aspartate residue of symmetry related molecules.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
