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Discrete Hybrid Vanadium-oxo Cluster as a Targeted Tool for Selective Protein Oxidative Modifications and Cleavage

Mhamad Aly Moussawi1, Francisco de Azambuja1, Tatjana N Parac-Vogt1

  • 1Department of Chemistry, KU Leuven, Celestijnenlaan 200F, 3001, Leuven, Belgium.

Angewandte Chemie (International Ed. in English)
|January 10, 2025
PubMed

Insights

A novel hybrid vanadate cluster, V6-OH, enables selective oxidative modification and cleavage of proteins under physiological conditions. This discovery offers new avenues for controlling protein damage and developing therapeutic strategies.

Area of Science:

  • Biochemistry
  • Materials Science
  • Chemical Biology

Background:

  • Oxidative modification of proteins is crucial for understanding cellular damage and death.
  • Selective induction of protein oxidative modifications under physiological conditions is a significant challenge.
  • Vanadium-based compounds show potential in biological applications but require precise control.

Purpose of the Study:

  • To demonstrate the use of a hybrid metal-oxo cluster, [V6O13{(OCH2)3CCH2OH}2]2- (V6-OH), for selective protein oxidative cleavage and modifications.
  • To investigate the interaction of V6-OH with proteins and its mechanism of redox activity.
  • To explore the potential of V6-OH in spatially controlled protein modification.

Main Methods:

  • Synthesis and characterization of the V6-OH hybrid metal-oxo cluster.
  • Co-crystallization of V6-OH with hen egg white lysozyme (HEWL).
  • Single Crystal X-ray Diffraction (SC-XRD) to determine complex structure.
  • Liquid Chromatography-Mass Spectrometry (LC-MS) for analyzing oxidative modifications.
  • Controlled induction of reactive oxygen species (ROS) in the presence of ascorbate (Asc).

Main Results:

  • The first example of a protein-bound hybrid vanadate cluster (V6-OH) was presented.
  • SC-XRD revealed specific binding of V6-OH to HEWL, influenced by both the inorganic core and organic ligands.
  • Selective oxidation or cleavage of HEWL was achieved under physiological conditions via ROS generation.
  • The outcome (oxidation vs. cleavage) was tunable by V6-OH concentration.
  • Oxidative modifications were spatially localized near cluster binding sites.

Conclusions:

  • Hybrid metal-oxo clusters, specifically V6-OH, can selectively modify proteins.
  • The redox activity of vanadium and cluster-protein interactions enable controlled oxidative reactions.
  • This approach offers precise spatial control over ROS production for protein modification.
  • The study advances understanding of vanadium in biological systems and highlights potential therapeutic applications.
Keywords:
hexavanadatehybrid-polyoxometalatemetal-oxo clusteroxidationprotein

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