Cu(II) binding by angiotensin II fragments: Asp-Arg-Val-Tyr-Ile-His and Arg-Val-Tyr-Ile-His. Competition between amino group and imidazole nitrogens in anchoring of metal ions

J Inorg Biochem. 1995 Mar;57(4):235-47. doi: 10.1016/0162-0134(94)00026-7.

Abstract

Potentiometric and spectroscopic (absorption, circular dichroism and electron paramagnetic resonance) study on the coordination of two angiotensin II fragments (Asp-Arg-Val-Tyr-Ile-His and Arg-Val-Tyr-Ile-His) to Cu(II) ions has shown that competition between amino and imidazole nitrogens to anchor metal ions is a complicated process and may lead to formation of macrochelate rings. The important factor that influences this competition is the distance between competing His and N-terminal residues (number of spacer residues in a peptide sequence).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Angiotensin II / chemistry
  • Angiotensin II / metabolism*
  • Binding, Competitive
  • Cations / metabolism
  • Circular Dichroism
  • Copper / metabolism*
  • Electron Spin Resonance Spectroscopy
  • Humans
  • Imidazoles / metabolism
  • Molecular Sequence Data
  • Nitrogen / metabolism
  • Peptide Fragments / metabolism*
  • Spectrophotometry

Substances

  • Cations
  • Imidazoles
  • Peptide Fragments
  • Angiotensin II
  • Copper
  • imidazole
  • Nitrogen