Jump to main content
Jump to site search

Issue 10, 2018
Previous Article Next Article

Complex formation of nickel(II) and zinc(II) ions with peptide fragments of rat amylin

Author affiliations

Abstract

Nickel(II) and zinc(II) complexes of the 19–22 peptide fragments of rat amylin were studied by potentiometric, UV-vis, CD and NMR spectroscopic methods. The results revealed that in contrast with the corresponding copper(II) complexes, the –SSNN– sequence (or 19–22 residues of rat amylin) cannot be the primary anchoring site for nickel(II) and zinc(II) ions. For nickel(II) containing systems, an increased stability of the corresponding complexes was, however, measured and explained by an equilibrium between the common (NH2,3N(peptide)) and (NH2,2N(peptide),N(asparagine)) coordination modes in a basic solution. From the comparison of the results obtained for the copper(II), nickel(II) and zinc(II) ions, it can be unambiguously stated that the rat amylin have an outstanding affinity for copper(II) binding.

Graphical abstract: Complex formation of nickel(ii) and zinc(ii) ions with peptide fragments of rat amylin

Back to tab navigation

Supplementary files

Publication details

The article was received on 24 Nov 2017, accepted on 06 Feb 2018 and first published on 06 Feb 2018


Article type: Paper
DOI: 10.1039/C7NJ04605G
Citation: New J. Chem., 2018,42, 8131-8136
  •   Request permissions

    Complex formation of nickel(II) and zinc(II) ions with peptide fragments of rat amylin

    Á. Dávid, É. T. Hartman, N. Lihi, I. Sóvágó and K. Várnagy, New J. Chem., 2018, 42, 8131
    DOI: 10.1039/C7NJ04605G

Search articles by author

Spotlight

Advertisements