Stabilization and Binding of [V4 O12 ]4- and Unprecedented [V20 O54 (NO3 )]n- to Lysozyme upon Loss of Ligands and Oxidation of the Potential Drug VIV O(acetylacetonato)2

Angew Chem Int Ed Engl. 2023 Dec 11;62(50):e202310655. doi: 10.1002/anie.202310655. Epub 2023 Oct 13.

Abstract

High-resolution crystal structures of lysozyme in the presence of the potential drug VIV O(acetylacetonato)2 under two different experimental conditions have been solved. The crystallographic study reveals the loss of the ligands, the oxidation of VIV to VV and the subsequent formation of adducts of the protein with two different polyoxidovanadates: [V4 O12 ]4- , which interacts with lysozyme non-covalently, and the unprecedented [V20 O54 (NO3 )]n- , which is covalenty bound to the side chain of an aspartate residue of symmetry related molecules.

Keywords: Lysozyme; Polyhedra; Polyoxidovanadates; Protein Interaction; Vanadium; Vanadium-Based Drugs.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Ligands
  • Muramidase* / chemistry
  • Oxidation-Reduction
  • Proteins*
  • Vanadium / chemistry

Substances

  • Muramidase
  • Proteins
  • Vanadium
  • Ligands