The role of the histidine residue in the coordination abilities of peptides with a multi-histidine sequence towards copper(II) ions

Agnieszka Matera, Justyna Brasuń, Marek Cebrat, Jolanta Światek-Kozłowska

Research output: Contribution to journalArticle

Abstract

Cu2+ complexes with peptides containing three histidine residues have very specific metal binding abilities and can mimic the structures of various multi-histidine metal binding sites in proteins. The main goal of the work concerns the investigations of coordination abilities of the group of N-terminally protected Ac-His-Arg-His-Gly-His-Gly, Ac-His-Gly-His-Arg-His-Gly, Ac-Gly-His-His-Arg-His-Gly and Ac-His-His-Gly-His-Arg-Gly, and their unprotected analogs His-Arg-His-Gly-His-Gly, His-Gly-His-Arg-His-Gly, Gly-His-His-Arg-His-Gly and His-His-Gly-His-Arg-Gly towards Cu2+ ions. Detailed spectroscopic (UV/Vis, CD and EPR) and potentiometric studies have been made. The stoichiometry and binding mode for each ligand-Cu2+ system were determined. In the case of N-terminally protected peptides the coordination begins at the imidazole nitrogen(s) which act as the anchoring groups. At physiological pH the {3Nim, 2N-} binding pattern is suggested and at high pH three amide nitrogens are involved in Cu2+ binding. According to the coordination abilities of the unprotected peptides, the position of the histidine residue determines the coordination mode. For His1 peptides the histamine-like {NH2, Nim} mode for the first species is suggested. The final albumin-like coordination mode is proposed not only for HGHRHG and HRHGHG but also for GHHRHG. For ligands with the His-Xaa-His motif the {2N-, 2Nim} binding mode is formed easier. For ligands with His2 the 3N complex with the {NH2, N-, Nim} binding pattern is a dominant species within the physiological pH range. The protection of the amine group caused a significant decrease of the coordination abilities of the peptides.

Original languageEnglish (US)
Pages (from-to)1539-1555
Number of pages17
JournalPolyhedron
Volume27
Issue number6
DOIs
StatePublished - Apr 25 2008
Externally publishedYes

Fingerprint

histidine
Histidine
Peptides
peptides
Copper
Ions
copper
Ligands
ions
Nitrogen
ligands
Metals
histamines
nitrogen
Binding sites
Amides
Stoichiometry
Histamine
Amines
Paramagnetic resonance

Keywords

  • Coordination chemistry
  • Copper (II)
  • Histidine
  • Peptides

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry
  • Physical and Theoretical Chemistry
  • Materials Chemistry

Cite this

The role of the histidine residue in the coordination abilities of peptides with a multi-histidine sequence towards copper(II) ions. / Matera, Agnieszka; Brasuń, Justyna; Cebrat, Marek; Światek-Kozłowska, Jolanta.

In: Polyhedron, Vol. 27, No. 6, 25.04.2008, p. 1539-1555.

Research output: Contribution to journalArticle

Matera, Agnieszka ; Brasuń, Justyna ; Cebrat, Marek ; Światek-Kozłowska, Jolanta. / The role of the histidine residue in the coordination abilities of peptides with a multi-histidine sequence towards copper(II) ions. In: Polyhedron. 2008 ; Vol. 27, No. 6. pp. 1539-1555.
@article{683aea1fb31146f3873acfd30c49b98e,
title = "The role of the histidine residue in the coordination abilities of peptides with a multi-histidine sequence towards copper(II) ions",
abstract = "Cu2+ complexes with peptides containing three histidine residues have very specific metal binding abilities and can mimic the structures of various multi-histidine metal binding sites in proteins. The main goal of the work concerns the investigations of coordination abilities of the group of N-terminally protected Ac-His-Arg-His-Gly-His-Gly, Ac-His-Gly-His-Arg-His-Gly, Ac-Gly-His-His-Arg-His-Gly and Ac-His-His-Gly-His-Arg-Gly, and their unprotected analogs His-Arg-His-Gly-His-Gly, His-Gly-His-Arg-His-Gly, Gly-His-His-Arg-His-Gly and His-His-Gly-His-Arg-Gly towards Cu2+ ions. Detailed spectroscopic (UV/Vis, CD and EPR) and potentiometric studies have been made. The stoichiometry and binding mode for each ligand-Cu2+ system were determined. In the case of N-terminally protected peptides the coordination begins at the imidazole nitrogen(s) which act as the anchoring groups. At physiological pH the {3Nim, 2N-} binding pattern is suggested and at high pH three amide nitrogens are involved in Cu2+ binding. According to the coordination abilities of the unprotected peptides, the position of the histidine residue determines the coordination mode. For His1 peptides the histamine-like {NH2, Nim} mode for the first species is suggested. The final albumin-like coordination mode is proposed not only for HGHRHG and HRHGHG but also for GHHRHG. For ligands with the His-Xaa-His motif the {2N-, 2Nim} binding mode is formed easier. For ligands with His2 the 3N complex with the {NH2, N-, Nim} binding pattern is a dominant species within the physiological pH range. The protection of the amine group caused a significant decrease of the coordination abilities of the peptides.",
keywords = "Coordination chemistry, Copper (II), Histidine, Peptides",
author = "Agnieszka Matera and Justyna Brasuń and Marek Cebrat and Jolanta Światek-Kozłowska",
year = "2008",
month = "4",
day = "25",
doi = "10.1016/j.poly.2007.12.035",
language = "English (US)",
volume = "27",
pages = "1539--1555",
journal = "Polyhedron",
issn = "0277-5387",
publisher = "Elsevier Limited",
number = "6",

}

TY - JOUR

T1 - The role of the histidine residue in the coordination abilities of peptides with a multi-histidine sequence towards copper(II) ions

AU - Matera, Agnieszka

AU - Brasuń, Justyna

AU - Cebrat, Marek

AU - Światek-Kozłowska, Jolanta

PY - 2008/4/25

Y1 - 2008/4/25

N2 - Cu2+ complexes with peptides containing three histidine residues have very specific metal binding abilities and can mimic the structures of various multi-histidine metal binding sites in proteins. The main goal of the work concerns the investigations of coordination abilities of the group of N-terminally protected Ac-His-Arg-His-Gly-His-Gly, Ac-His-Gly-His-Arg-His-Gly, Ac-Gly-His-His-Arg-His-Gly and Ac-His-His-Gly-His-Arg-Gly, and their unprotected analogs His-Arg-His-Gly-His-Gly, His-Gly-His-Arg-His-Gly, Gly-His-His-Arg-His-Gly and His-His-Gly-His-Arg-Gly towards Cu2+ ions. Detailed spectroscopic (UV/Vis, CD and EPR) and potentiometric studies have been made. The stoichiometry and binding mode for each ligand-Cu2+ system were determined. In the case of N-terminally protected peptides the coordination begins at the imidazole nitrogen(s) which act as the anchoring groups. At physiological pH the {3Nim, 2N-} binding pattern is suggested and at high pH three amide nitrogens are involved in Cu2+ binding. According to the coordination abilities of the unprotected peptides, the position of the histidine residue determines the coordination mode. For His1 peptides the histamine-like {NH2, Nim} mode for the first species is suggested. The final albumin-like coordination mode is proposed not only for HGHRHG and HRHGHG but also for GHHRHG. For ligands with the His-Xaa-His motif the {2N-, 2Nim} binding mode is formed easier. For ligands with His2 the 3N complex with the {NH2, N-, Nim} binding pattern is a dominant species within the physiological pH range. The protection of the amine group caused a significant decrease of the coordination abilities of the peptides.

AB - Cu2+ complexes with peptides containing three histidine residues have very specific metal binding abilities and can mimic the structures of various multi-histidine metal binding sites in proteins. The main goal of the work concerns the investigations of coordination abilities of the group of N-terminally protected Ac-His-Arg-His-Gly-His-Gly, Ac-His-Gly-His-Arg-His-Gly, Ac-Gly-His-His-Arg-His-Gly and Ac-His-His-Gly-His-Arg-Gly, and their unprotected analogs His-Arg-His-Gly-His-Gly, His-Gly-His-Arg-His-Gly, Gly-His-His-Arg-His-Gly and His-His-Gly-His-Arg-Gly towards Cu2+ ions. Detailed spectroscopic (UV/Vis, CD and EPR) and potentiometric studies have been made. The stoichiometry and binding mode for each ligand-Cu2+ system were determined. In the case of N-terminally protected peptides the coordination begins at the imidazole nitrogen(s) which act as the anchoring groups. At physiological pH the {3Nim, 2N-} binding pattern is suggested and at high pH three amide nitrogens are involved in Cu2+ binding. According to the coordination abilities of the unprotected peptides, the position of the histidine residue determines the coordination mode. For His1 peptides the histamine-like {NH2, Nim} mode for the first species is suggested. The final albumin-like coordination mode is proposed not only for HGHRHG and HRHGHG but also for GHHRHG. For ligands with the His-Xaa-His motif the {2N-, 2Nim} binding mode is formed easier. For ligands with His2 the 3N complex with the {NH2, N-, Nim} binding pattern is a dominant species within the physiological pH range. The protection of the amine group caused a significant decrease of the coordination abilities of the peptides.

KW - Coordination chemistry

KW - Copper (II)

KW - Histidine

KW - Peptides

UR - http://www.scopus.com/inward/record.url?scp=41349087691&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=41349087691&partnerID=8YFLogxK

U2 - 10.1016/j.poly.2007.12.035

DO - 10.1016/j.poly.2007.12.035

M3 - Article

AN - SCOPUS:41349087691

VL - 27

SP - 1539

EP - 1555

JO - Polyhedron

JF - Polyhedron

SN - 0277-5387

IS - 6

ER -