Metal Modulation of Oxytocin Structure, Function, and Receptor Interactions.

Oxytocin is a nine-amino acid peptide hormone essential for reproduction, social bonding, and neuromodulation. Accumulating evidence demonstrates that divalent metal ions play critical roles in modulating oxytocin structure, receptor binding, and biological activity. Despite nearly five decades of research, a comprehensive molecular-level understanding of metal-oxytocin interactions and their functional consequences remains incomplete. This review synthesizes current knowledge of how Cu2+, Zn2+, Mg2+, Ca2+, and other metals influence oxytocin's conformational landscape and receptor interactions through distinct coordination modes. We highlight emerging applications in biosensor development and therapeutic formulation that leverage these metal-binding properties. Advancing our understanding of metal-mediated modulation of oxytocin function will enhance our knowledge of peptide hormone regulation and provide new avenues for therapeutic intervention in conditions involving dysregulated oxytocin signaling.