The binding abilities of homodetic cyclic His-peptides toward copper ions

Aleksandra Kotynia, J. Pap, Justyna Brasun

Research output: Contribution to journalReview article

1 Citation (Scopus)

Abstract

The biochemistry of copper is important and worthy to be broadly studied. In biological systems copper is usually bound by enzymes, proteins or peptides and the investigation of the occurring interactions is still a hot topic. In this overview we focus on the copper binding abilities of homodetic cyclic peptides (CPs) containing histidine moieties. This group of ligands is characterized by a cyclic ring composed only of amino acids. Several applications of cyclic peptides should be viable because of their special structures, stability and resistance against enzymatic degradation. The cyclic structure promotes the anchoring of metal ions by the amino acid side chains. We discuss the impact of peptide cyclization and ring size on the binding abilities toward copper(II) ions. We also compare the coordinating properties of ligands containing a different number of His residues with the –(HX)n motif, where X = Gly, Lys, Arg, Asn or Pro, based on the stability constants of nNIm (n = 2–4) complexes created by His4-cyclopeptides. In addition, we compare the sustainability and stability of nNIm (n = 1–4) complexes depending on the Asp residue in the peptide sequence and we also consider the aspects of forming dinuclear copper(II) complexes by cyclopeptides with two separated Pro residues in the sequence. The di-Cu(II)-complexes are favored in the basic pH range. So far, cyclopeptides found use in pharmaceutical chemistry, biochemistry, and life sciences, but also as ionophores and nano-materials. We advocate here to use their metal ion complexes because they enrich the spectrum of available activities of metallopeptides or change the properties of these ligands.

Original languageEnglish
Pages (from-to)3-11
Number of pages9
JournalInorganica Chimica Acta
Volume472
DOIs
Publication statusPublished - Mar 1 2018

Fingerprint

Cyclic Peptides
Peptides
peptides
Copper
Ions
copper
biochemistry
Biochemistry
Ligands
ions
ligands
Metal ions
amino acids
Amino acids
metal ions
Ionophores
Amino Acids
life sciences
histidine
rings

Keywords

  • Complex
  • Copper
  • Cyclic peptide
  • Histidine
  • Stability constant

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Inorganic Chemistry
  • Materials Chemistry

Cite this

The binding abilities of homodetic cyclic His-peptides toward copper ions. / Kotynia, Aleksandra; Pap, J.; Brasun, Justyna.

In: Inorganica Chimica Acta, Vol. 472, 01.03.2018, p. 3-11.

Research output: Contribution to journalReview article

Kotynia, Aleksandra ; Pap, J. ; Brasun, Justyna. / The binding abilities of homodetic cyclic His-peptides toward copper ions. In: Inorganica Chimica Acta. 2018 ; Vol. 472. pp. 3-11.
@article{213b8b22ed4e4688bdc7ffb14c1b6b50,
title = "The binding abilities of homodetic cyclic His-peptides toward copper ions",
abstract = "The biochemistry of copper is important and worthy to be broadly studied. In biological systems copper is usually bound by enzymes, proteins or peptides and the investigation of the occurring interactions is still a hot topic. In this overview we focus on the copper binding abilities of homodetic cyclic peptides (CPs) containing histidine moieties. This group of ligands is characterized by a cyclic ring composed only of amino acids. Several applications of cyclic peptides should be viable because of their special structures, stability and resistance against enzymatic degradation. The cyclic structure promotes the anchoring of metal ions by the amino acid side chains. We discuss the impact of peptide cyclization and ring size on the binding abilities toward copper(II) ions. We also compare the coordinating properties of ligands containing a different number of His residues with the –(HX)n − motif, where X = Gly, Lys, Arg, Asn or Pro, based on the stability constants of nNIm (n = 2–4) complexes created by His4-cyclopeptides. In addition, we compare the sustainability and stability of nNIm (n = 1–4) complexes depending on the Asp residue in the peptide sequence and we also consider the aspects of forming dinuclear copper(II) complexes by cyclopeptides with two separated Pro residues in the sequence. The di-Cu(II)-complexes are favored in the basic pH range. So far, cyclopeptides found use in pharmaceutical chemistry, biochemistry, and life sciences, but also as ionophores and nano-materials. We advocate here to use their metal ion complexes because they enrich the spectrum of available activities of metallopeptides or change the properties of these ligands.",
keywords = "Complex, Copper, Cyclic peptide, Histidine, Stability constant",
author = "Aleksandra Kotynia and J. Pap and Justyna Brasun",
year = "2018",
month = "3",
day = "1",
doi = "10.1016/j.ica.2017.07.028",
language = "English",
volume = "472",
pages = "3--11",
journal = "Inorganica Chimica Acta",
issn = "0020-1693",
publisher = "Elsevier BV",

}

TY - JOUR

T1 - The binding abilities of homodetic cyclic His-peptides toward copper ions

AU - Kotynia, Aleksandra

AU - Pap, J.

AU - Brasun, Justyna

PY - 2018/3/1

Y1 - 2018/3/1

N2 - The biochemistry of copper is important and worthy to be broadly studied. In biological systems copper is usually bound by enzymes, proteins or peptides and the investigation of the occurring interactions is still a hot topic. In this overview we focus on the copper binding abilities of homodetic cyclic peptides (CPs) containing histidine moieties. This group of ligands is characterized by a cyclic ring composed only of amino acids. Several applications of cyclic peptides should be viable because of their special structures, stability and resistance against enzymatic degradation. The cyclic structure promotes the anchoring of metal ions by the amino acid side chains. We discuss the impact of peptide cyclization and ring size on the binding abilities toward copper(II) ions. We also compare the coordinating properties of ligands containing a different number of His residues with the –(HX)n − motif, where X = Gly, Lys, Arg, Asn or Pro, based on the stability constants of nNIm (n = 2–4) complexes created by His4-cyclopeptides. In addition, we compare the sustainability and stability of nNIm (n = 1–4) complexes depending on the Asp residue in the peptide sequence and we also consider the aspects of forming dinuclear copper(II) complexes by cyclopeptides with two separated Pro residues in the sequence. The di-Cu(II)-complexes are favored in the basic pH range. So far, cyclopeptides found use in pharmaceutical chemistry, biochemistry, and life sciences, but also as ionophores and nano-materials. We advocate here to use their metal ion complexes because they enrich the spectrum of available activities of metallopeptides or change the properties of these ligands.

AB - The biochemistry of copper is important and worthy to be broadly studied. In biological systems copper is usually bound by enzymes, proteins or peptides and the investigation of the occurring interactions is still a hot topic. In this overview we focus on the copper binding abilities of homodetic cyclic peptides (CPs) containing histidine moieties. This group of ligands is characterized by a cyclic ring composed only of amino acids. Several applications of cyclic peptides should be viable because of their special structures, stability and resistance against enzymatic degradation. The cyclic structure promotes the anchoring of metal ions by the amino acid side chains. We discuss the impact of peptide cyclization and ring size on the binding abilities toward copper(II) ions. We also compare the coordinating properties of ligands containing a different number of His residues with the –(HX)n − motif, where X = Gly, Lys, Arg, Asn or Pro, based on the stability constants of nNIm (n = 2–4) complexes created by His4-cyclopeptides. In addition, we compare the sustainability and stability of nNIm (n = 1–4) complexes depending on the Asp residue in the peptide sequence and we also consider the aspects of forming dinuclear copper(II) complexes by cyclopeptides with two separated Pro residues in the sequence. The di-Cu(II)-complexes are favored in the basic pH range. So far, cyclopeptides found use in pharmaceutical chemistry, biochemistry, and life sciences, but also as ionophores and nano-materials. We advocate here to use their metal ion complexes because they enrich the spectrum of available activities of metallopeptides or change the properties of these ligands.

KW - Complex

KW - Copper

KW - Cyclic peptide

KW - Histidine

KW - Stability constant

UR - http://www.scopus.com/inward/record.url?scp=85025695246&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85025695246&partnerID=8YFLogxK

U2 - 10.1016/j.ica.2017.07.028

DO - 10.1016/j.ica.2017.07.028

M3 - Review article

AN - SCOPUS:85025695246

VL - 472

SP - 3

EP - 11

JO - Inorganica Chimica Acta

JF - Inorganica Chimica Acta

SN - 0020-1693

ER -