A potentiometric and spectroscopic study of the interaction of the N terminal tetrapeptide fragment of fibrinopeptide A with Cu II and Ni II
- 1 January 1986
- journal article
- research article
- Published by Royal Society of Chemistry (RSC) in J. Chem. Soc., Dalton Trans.
- No. 10,p. 2221-2226
- https://doi.org/10.1039/dt9860002221
Abstract
The syntheses are reported of the amino-terminal tetrapeptide fragment of human fibrinopeptide A (Ala-Asp-Ser-Gly) and derivative tetrapeptides with the β-carboxylate of the aspartate residue and the hydroxy group of the serine residue blocked to prevent co-ordination to metal ions. Complexes with hydrogen ion and copper(II), and in the case of Ala-Asp-Ser-Gly with nickel(II) also, have been studied by a combined approach of potentiometric and spectroscopic [absorption, circular dichroism, e.s.r. and, with nickel(II), 1H n.m.r.] techniques. Stability constants of copper(II) and nickel(II) complexes of ‘tetra-alanine’(Ala-Ala-Ala-Ala) have also been measured. The β-carboxylate group has been shown to co-ordinate strongly to CuII over the pH range 4–9 to give an unusually stable [CuH–1L] species (overall charge omitted). Fibrinopeptide A, which is present in locally high concentrations near the sites of bodily injury, would similarly be expected to co-ordinate strongly to CuII.Keywords
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