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

Israel Alshanski; Deborah E. Shalev; Shlomo Yitzchaik; Mattan Hurevich

doi:10.1007/s00775-021-01897-1

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

Israel Alshanski, Deborah E. Shalev, Shlomo Yitzchaik, Mattan Hurevich

The Hebrew University of Jerusalem

Research output: Contribution to journal › Article › peer-review

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⁺. Graphic abstract: [Figure not available: see fulltext.]

Original language	English
Pages (from-to)	809-815
Number of pages	7
Journal	Journal of Biological Inorganic Chemistry
Volume	26
Issue number	7
DOIs	https://doi.org/10.1007/s00775-021-01897-1
State	Published - Oct 2021

Keywords

Copper complex
Nuclear magnetic resonance
Oxytocin
Paramagnetic resonance enhancement
Peptide

All Science Journal Classification (ASJC) codes

Biochemistry
Inorganic Chemistry

Access to Document

10.1007/s00775-021-01897-1

Cite this

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

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+. Graphic abstract: [Figure not available: see fulltext.]",

keywords = "Copper complex, Nuclear magnetic resonance, Oxytocin, Paramagnetic resonance enhancement, Peptide",

author = "Israel Alshanski and Shalev, {Deborah E.} and Shlomo Yitzchaik and Mattan Hurevich",

note = "Publisher Copyright: {\textcopyright} 2021, Society for Biological Inorganic Chemistry (SBIC).",

year = "2021",

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T1 - Determining the structure and binding mechanism of oxytocin-Cu2+ complex using paramagnetic relaxation enhancement NMR analysis

AU - Alshanski, Israel

AU - Shalev, Deborah E.

AU - Yitzchaik, Shlomo

AU - Hurevich, Mattan

PY - 2021/10

Y1 - 2021/10

N2 - 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.]

AB - 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.]

KW - Copper complex

KW - Nuclear magnetic resonance

KW - Oxytocin

KW - Paramagnetic resonance enhancement

KW - Peptide

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DO - 10.1007/s00775-021-01897-1

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SN - 0949-8257

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SP - 809

EP - 815

JO - Journal of Biological Inorganic Chemistry

JF - Journal of Biological Inorganic Chemistry

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