Zn(2+)-induced deprotonation of a peptide nitrogen in angiotensin I

A P Arnold; D M Stanley; J G Collins

doi:10.1016/0014-5793(91)80916-q

Zn(2+)-induced deprotonation of a peptide nitrogen in angiotensin I

FEBS Lett. 1991 Sep 2;289(1):96-8. doi: 10.1016/0014-5793(91)80916-q.

Authors

A P Arnold¹, D M Stanley, J G Collins

Affiliation

¹ Department of Chemistry, University College, University of New South Wales, Australian Defence Force Academy.

PMID: 1654278
DOI: 10.1016/0014-5793(91)80916-q

Abstract

The interaction of Zn2+ with angiotensin I, a decapeptide containing two histidyl residues, has been studied by 1H-NMR spectroscopy in both water and dimethylsulfoxide. When Zn2+ is added to the peptide in dimethylsulfoxide, binding occurs by coordination of the imidazole rings of both histidines to the metal-ion, enabling the deprotonation of the Phe peptide nitrogen.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Angiotensin I / chemistry*
Magnetic Resonance Spectroscopy
Molecular Sequence Data
Nitrogen / chemistry*
Peptides / chemistry
Protons
Zinc / chemistry*

Substances

Peptides
Protons
Angiotensin I
Zinc
Nitrogen