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.
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).
Bal
W
W
Institute of Chemistry, University of Wroclaw, Poland.
Jezowska-Bojczuk
M
M
Kozlowski
H
H
Chruscinski
L
L
Kupryszewski
G
G
Witczuk
B
B
D000595:Amino Acid Sequence; D000804:Angiotensin II / Q000737:chemistry / Q000378:metabolism*; D001667:Binding, Competitive; D002412:Cations / Q000378:metabolism; D002942:Circular Dichroism; D003300:Copper / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy; D006801:Humans; D007093:Imidazoles / Q000378:metabolism; D008969:Molecular Sequence Data; D009584:Nitrogen / Q000378:metabolism; D010446:Peptide Fragments / Q000378:metabolism*; D013053:Spectrophotometry
D002412:Cations; D007093:Imidazoles; D010446:Peptide Fragments; D000804:Angiotensin II; D003300:Copper; C029899:imidazole; D009584:Nitrogen