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Determining the structure and binding mechanism of oxytocin-Cu2+ complex using paramagnetic relaxation enhancement NMR analysis

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Abstract

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+.

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Oxytocin copper complex structure revealed by paramagnetic relaxation enhancement NMR analyses

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Acknowledgements

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.

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Authors and Affiliations

  1. Institute of Chemistry and Center for Nanoscience and Nanotechnology, The Hebrew University of Jerusalem, Edmond J. Safra Campus, Givat Ram, 91904, Jerusalem, Israel

    Israel Alshanski, Shlomo Yitzchaik & Mattan Hurevich

  2. Department of Pharmaceutical Engineering, Azrieli College of Engineering Jerusalem, 91035, Jerusalem, Israel

    Deborah E. Shalev

  3. Wolfson Centre for Applied Structural Biology, The Hebrew University of Jerusalem, Edmond J. Safra Campus, Givat Ram, 91904, Jerusalem, Israel

    Deborah E. Shalev

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  1. Israel Alshanski
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  2. Deborah E. Shalev
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Correspondence to Deborah E. Shalev, Shlomo Yitzchaik or Mattan Hurevich.

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Alshanski, I., Shalev, D.E., Yitzchaik, S. et al. Determining the structure and binding mechanism of oxytocin-Cu2+ complex using paramagnetic relaxation enhancement NMR analysis. J Biol Inorg Chem 26, 809–815 (2021). https://doi.org/10.1007/s00775-021-01897-1

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