Oxytocin is a neuropeptide that binds copper ions in nature. The structure of oxytocin in interaction with Cu2+ was determined here by NMR, showing which atoms of the peptide are involved in binding. Paramagnetic relaxation enhancement NMR analyses indicated a binding mechanism where the amino terminus was required for binding and subsequently Tyr2, Ile3 and Gln4 bound in that order. The aromatic ring of Tyr2 formed a π-cation interaction with Cu2+. Graphic abstract: [Figure not available: see fulltext.]
Bibliographical noteFunding Information:
The authors would like to thank RECORD-IT project. This project has received funding from the European Union’s Horizon 2020 research and innovation programme under grant agreement No 664786; SY is the Benjamin H. Birstein Chair in Chemistry. IA is supported by a Hebrew University Center for Nanoscience and Nanotechnology Ph.D. scholarship.
© 2021, Society for Biological Inorganic Chemistry (SBIC).
- Copper complex
- Nuclear magnetic resonance
- Paramagnetic resonance enhancement