Zn2+‐induced deprotonation of a peptide nitrogen in angiotensin I

FEBS Letters

Arnold, Alan P.¹  Collins, J.Grant¹  Stanley, Darren M.¹ 

[1] Department of Chemistry, University College, University of New South Wales, Australian Defence Force Academy, A.C.T. 2600, Australia

关键词: 1H-NMR;    Zinc binding;    Deprotonated amide;    Angiotensin I;    Peptide;   

DOI  :  10.1016/0014-5793(91)80916-Q

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown