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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\u2010level understanding of metal\u2013oxytocin interactions and their functional consequences remains incomplete. This review synthesizes current knowledge of how Cu\n                    <jats:sup>2+<\/jats:sup>\n                    , Zn\n                    <jats:sup>2+<\/jats:sup>\n                    , Mg\n                    <jats:sup>2+<\/jats:sup>\n                    , Ca\n                    <jats:sup>2+<\/jats:sup>\n                    , 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\u2010binding properties. Advancing our understanding of metal\u2010mediated 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.\n                  <\/jats:p>","DOI":"10.1002\/ejic.202500462","type":"journal-article","created":{"date-parts":[[2026,4,6]],"date-time":"2026-04-06T13:40:32Z","timestamp":1775482832000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Metal Modulation of Oxytocin Structure, Function, and Receptor Interactions"],"prefix":"10.1002","volume":"29","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-1544-2971","authenticated-orcid":false,"given":"Jennifer","family":"Park","sequence":"first","affiliation":[{"name":"Department of Chemistry University of California Davis  Davis California 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