Complex formation of nickel(II) and zinc(II) ions with peptide fragments of rat amylin (vol 42, pg 8131, 2018)

被引：0

作者：

David, Agnes ^{[1
]}

Hartman, Eva Tunde ^{[1
]}

Lihi, Norbert ^{[2
]}

Sovago, Imre ^{[1
]}

Varnagy, Katalin ^{[1
]}

机构：

[1] Univ Debrecen, Dept Inorgan & Analyt Chem, Egyet Ter 1, H-4032 Debrecen, Hungary

[2] Univ Debrecen, MTA DE Redox & Homogeneous Catalyt React Mech Res, Egyet Ter 1, H-4032 Debrecen, Hungary

来源：

NEW JOURNAL OF CHEMISTRY | 2018年 / 42卷 / 10期

基金：

匈牙利科学研究基金会;

关键词：

D O I：

10.1039/c8nj90036a

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

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.

引用

页码：8277 / 8277

页数：1