Nickel(II), zinc(II) and cadmium(II) complexes of peptides containing separate aspartyl and cysteinyl residues

Norbert Lihi, Márton Lukács, Dóra Szűcs, K. Várnagy, I. Sóvágó

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Nickel(II), zinc(II) and cadmium(II) complexes of two hexapeptides ADAAAC-NH2 and AADAAC-NH2 containing terminal amino, separate aspartyl carboxylate and cysteinyl thiolate donor functions have been studied by potentiometric and spectroscopic techniques. For nickel(II), the amino terminus and the aspartyl residues are the primary metal binding sites. At high pH values, thiolate groups can also coordinate to nickel(II) and this interaction results in the co-existence of various coordination isomers. In the case of AADAAC-NH2, even dinuclear complexes can be formed with separate (NH2, N, N, COO) and (S, 3N) binding modes. On the contrary, the thiolate functions are the primary binding site for zinc(II) and especially cadmium(II) ions. The formation of macrochelate complexes is the most characteristic with these metal ions including the terminal amino, the internal carboxylate and thiolate donor functions. None of the side chain donors can, however, induce the deprotonation and zinc(II) or cadmium(II) coordination of the amide functions of these peptides.

Original languageEnglish
Pages (from-to)364-373
Number of pages10
JournalPolyhedron
Volume133
DOIs
Publication statusPublished - Sep 5 2017

Fingerprint

Nickel
Cadmium
cadmium
Peptides
peptides
Zinc
zinc
nickel
Binding sites
carboxylates
Binding Sites
Deprotonation
Amides
Isomers
amides
Metal ions
metal ions
isomers
Metals
Ions

Keywords

  • Cadmium(II)
  • Complexes
  • Nickel(II)
  • Peptides
  • Zinc(II)

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Inorganic Chemistry
  • Materials Chemistry

Cite this

Nickel(II), zinc(II) and cadmium(II) complexes of peptides containing separate aspartyl and cysteinyl residues. / Lihi, Norbert; Lukács, Márton; Szűcs, Dóra; Várnagy, K.; Sóvágó, I.

In: Polyhedron, Vol. 133, 05.09.2017, p. 364-373.

Research output: Contribution to journalArticle

@article{79131f2119bd4b5fa8df99ae53186ac3,
title = "Nickel(II), zinc(II) and cadmium(II) complexes of peptides containing separate aspartyl and cysteinyl residues",
abstract = "Nickel(II), zinc(II) and cadmium(II) complexes of two hexapeptides ADAAAC-NH2 and AADAAC-NH2 containing terminal amino, separate aspartyl carboxylate and cysteinyl thiolate donor functions have been studied by potentiometric and spectroscopic techniques. For nickel(II), the amino terminus and the aspartyl residues are the primary metal binding sites. At high pH values, thiolate groups can also coordinate to nickel(II) and this interaction results in the co-existence of various coordination isomers. In the case of AADAAC-NH2, even dinuclear complexes can be formed with separate (NH2, N−, N−, COO−) and (S−, 3N−) binding modes. On the contrary, the thiolate functions are the primary binding site for zinc(II) and especially cadmium(II) ions. The formation of macrochelate complexes is the most characteristic with these metal ions including the terminal amino, the internal carboxylate and thiolate donor functions. None of the side chain donors can, however, induce the deprotonation and zinc(II) or cadmium(II) coordination of the amide functions of these peptides.",
keywords = "Cadmium(II), Complexes, Nickel(II), Peptides, Zinc(II)",
author = "Norbert Lihi and M{\'a}rton Luk{\'a}cs and D{\'o}ra Szűcs and K. V{\'a}rnagy and I. S{\'o}v{\'a}g{\'o}",
year = "2017",
month = "9",
day = "5",
doi = "10.1016/j.poly.2017.05.044",
language = "English",
volume = "133",
pages = "364--373",
journal = "Polyhedron",
issn = "0277-5387",
publisher = "Elsevier Limited",

}

TY - JOUR

T1 - Nickel(II), zinc(II) and cadmium(II) complexes of peptides containing separate aspartyl and cysteinyl residues

AU - Lihi, Norbert

AU - Lukács, Márton

AU - Szűcs, Dóra

AU - Várnagy, K.

AU - Sóvágó, I.

PY - 2017/9/5

Y1 - 2017/9/5

N2 - Nickel(II), zinc(II) and cadmium(II) complexes of two hexapeptides ADAAAC-NH2 and AADAAC-NH2 containing terminal amino, separate aspartyl carboxylate and cysteinyl thiolate donor functions have been studied by potentiometric and spectroscopic techniques. For nickel(II), the amino terminus and the aspartyl residues are the primary metal binding sites. At high pH values, thiolate groups can also coordinate to nickel(II) and this interaction results in the co-existence of various coordination isomers. In the case of AADAAC-NH2, even dinuclear complexes can be formed with separate (NH2, N−, N−, COO−) and (S−, 3N−) binding modes. On the contrary, the thiolate functions are the primary binding site for zinc(II) and especially cadmium(II) ions. The formation of macrochelate complexes is the most characteristic with these metal ions including the terminal amino, the internal carboxylate and thiolate donor functions. None of the side chain donors can, however, induce the deprotonation and zinc(II) or cadmium(II) coordination of the amide functions of these peptides.

AB - Nickel(II), zinc(II) and cadmium(II) complexes of two hexapeptides ADAAAC-NH2 and AADAAC-NH2 containing terminal amino, separate aspartyl carboxylate and cysteinyl thiolate donor functions have been studied by potentiometric and spectroscopic techniques. For nickel(II), the amino terminus and the aspartyl residues are the primary metal binding sites. At high pH values, thiolate groups can also coordinate to nickel(II) and this interaction results in the co-existence of various coordination isomers. In the case of AADAAC-NH2, even dinuclear complexes can be formed with separate (NH2, N−, N−, COO−) and (S−, 3N−) binding modes. On the contrary, the thiolate functions are the primary binding site for zinc(II) and especially cadmium(II) ions. The formation of macrochelate complexes is the most characteristic with these metal ions including the terminal amino, the internal carboxylate and thiolate donor functions. None of the side chain donors can, however, induce the deprotonation and zinc(II) or cadmium(II) coordination of the amide functions of these peptides.

KW - Cadmium(II)

KW - Complexes

KW - Nickel(II)

KW - Peptides

KW - Zinc(II)

UR - http://www.scopus.com/inward/record.url?scp=85020861340&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85020861340&partnerID=8YFLogxK

U2 - 10.1016/j.poly.2017.05.044

DO - 10.1016/j.poly.2017.05.044

M3 - Article

AN - SCOPUS:85020861340

VL - 133

SP - 364

EP - 373

JO - Polyhedron

JF - Polyhedron

SN - 0277-5387

ER -