A potentiometric and spectroscopic study of the proton, and copper (II) and zinc (II) complexes formed by fibrinopeptide A.
Results are reported for a potentiometric and spectroscopic (visible, CD, and EPR) study of the complexes of fibrinopeptide A (Ala-Asp-Ser-Gly-Glu-Gly-Asp-Phe-Leu-Ala-Glu-Gly-Gly-Gly-Val-Arg) with H+, Cu2+ and Zn2+. They show that the peptide forms stable complexes with Cu2+, largely as a result of the Asp2 residue, and that its coordination behavior is almost identical to that of the N-terminal tetrapeptide fragment, Ala-Asp-Ser-Gly. Hence the influence of the remaining amino acid residues on coordination to Cu2+ is insignificant.
Galey
J F
JF
Laboratoire de Chimie Macromoleculaire, Université des Sciences et Techniques de Lille, France.
Kozlowski
H
H
Pettit
L D
LD
D000595:Amino Acid Sequence; D003300:Copper / Q000737:chemistry; D005344:Fibrinopeptide A / Q000737:chemistry*; D006801:Humans; D008969:Molecular Sequence Data; D011199:Potentiometry; D011522:Protons; D013053:Spectrophotometry; D015032:Zinc / Q000737:chemistry
D011522:Protons; D005344:Fibrinopeptide A; D003300:Copper; D015032:Zinc