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

Ágnes Dávid, Éva Tünde Hartman, Norbert Lihi, I. Sóvágó, K. Várnagy

Research output: Contribution to journalArticle

2 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)8131-8136
Number of pages6
JournalNew Journal of Chemistry
Volume42
Issue number10
DOIs
Publication statusPublished - Jan 1 2018

Fingerprint

Islet Amyloid Polypeptide
Peptide Fragments
Nickel
Peptides
Zinc
Rats
Ions
Copper
Asparagine
Nuclear magnetic resonance

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Materials Chemistry

Cite this

Complex formation of nickel(ii) and zinc(ii) ions with peptide fragments of rat amylin. / Dávid, Ágnes; Hartman, Éva Tünde; Lihi, Norbert; Sóvágó, I.; Várnagy, K.

In: New Journal of Chemistry, Vol. 42, No. 10, 01.01.2018, p. 8131-8136.

Research output: Contribution to journalArticle

Dávid, Ágnes ; Hartman, Éva Tünde ; Lihi, Norbert ; Sóvágó, I. ; Várnagy, K. / Complex formation of nickel(ii) and zinc(ii) ions with peptide fragments of rat amylin. In: New Journal of Chemistry. 2018 ; Vol. 42, No. 10. pp. 8131-8136.
@article{73453a0fcf3b468bb696d79fe4cbe08f,
title = "Complex formation of nickel(ii) and zinc(ii) ions with peptide fragments of rat amylin",
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.",
author = "{\'A}gnes D{\'a}vid and Hartman, {{\'E}va T{\"u}nde} and Norbert Lihi and I. S{\'o}v{\'a}g{\'o} and K. V{\'a}rnagy",
year = "2018",
month = "1",
day = "1",
doi = "10.1039/c7nj04605g",
language = "English",
volume = "42",
pages = "8131--8136",
journal = "New Journal of Chemistry",
issn = "1144-0546",
publisher = "Royal Society of Chemistry",
number = "10",

}

TY - JOUR

T1 - Complex formation of nickel(ii) and zinc(ii) ions with peptide fragments of rat amylin

AU - Dávid, Ágnes

AU - Hartman, Éva Tünde

AU - Lihi, Norbert

AU - Sóvágó, I.

AU - Várnagy, K.

PY - 2018/1/1

Y1 - 2018/1/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=85047019277&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85047019277&partnerID=8YFLogxK

U2 - 10.1039/c7nj04605g

DO - 10.1039/c7nj04605g

M3 - Article

VL - 42

SP - 8131

EP - 8136

JO - New Journal of Chemistry

JF - New Journal of Chemistry

SN - 1144-0546

IS - 10

ER -