@article { WOS:000691234500002, title = {Determining the structure and binding mechanism of oxytocin-Cu2+ complex using paramagnetic relaxation enhancement NMR analysis}, journal = {JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY}, volume = {26}, year = {2021}, note = {[[{"fid":"256176","view_mode":"default","type":"media","attributes":{"style":"width: 300px; height: 160px;","alt":"123","class":"img-responsive media-element file-default"}}]]}, month = {OCT}, pages = {809-815}, 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 pi-cation interaction with Cu2+Y.\ 


}, issn = {0949-8257}, doi = {10.1007/s00775-021-01897-1}, author = {Alshanski, Israel and Deborah E. Shalev and Yitzchaik, Shlomo and Mattan Hurevich} }