Intracellular proteins with metal-chelating residues

Intracellular proteins with metal-chelating residues refers to a broad class of proteins that possess amino acid side chains, such as histidine, cysteine, aspartate, or glutamate, capable of coordinating metal ions like iron, copper, or zinc (UniProt, 2024). These proteins play critical roles in cellular processes including enzymatic catalysis, structural stability, and metal ion homeostasis (PubMed, 2023). In a pharmacological context, this term is often used to describe the collective target of intracellular chelating agents like dexrazoxane (DrugBank, DB00380). By binding to the metal ions associated with these proteins, such drugs prevent the formation of toxic metal-drug complexes, such as iron-anthracycline complexes, and the subsequent generation of reactive oxygen species (StatPearls, NBK559245). This mechanism is primarily utilized to mitigate oxidative stress-induced damage, such as the cardiotoxicity associated with certain chemotherapeutic agents (NIH, 2023). Consequently, while not a single molecular entity, these proteins represent a significant site for therapeutic intervention in managing metal-mediated toxicity and oxidative injury.

Other names

Intracellular metalloproteinsMetal-binding proteinsIntracellular metal-coordinating proteins

Chelation of intracellular metal ions (primarily iron) to prevent the formation of metal-anthracycline complexes and subsequent reactive oxygen species (ROS) generation.