New insights into the metal ion-peptide hydroxamate interactions

Metal complexes of primary hydroxamic acid derivatives of common dipeptides in aqueous solution

P. Buglyó, Eszter Márta Nagy, E. Farkas, I. Sóvágó, Daniele Sanna, Giovanni Micera

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

Complex formation of primary dipeptide hydroxamic acids, L-Ala-L-AlaNHOH and L-Ala-L-SerNHOH, as well as the corresponding Z-protected ones, Z-L-Ala-L-AlaNHOH and Z-L-Ala-L-SerNHOH (Z = benzyloxycarbonyl), with iron(III), aluminium(III), nickel(II), copper(II) and zinc(II) was studied in aqueous solution by pH-potentiometric and spectroscopic (UV-Vis, EPR, CD, 1H NMR) methods. The exclusive formation of [O,O] chelated hydroxamate complexes was found with iron(III) and aluminium(III) with all the ligands. Formation of linkage isomers with the involvement of either [O,O] hydroxamate or [NH2,CO] chelates was detected both in the zinc(II)-L-Ala-L-AlaNHOH and -L-Ala-L-SerNHOH systems. Upon increasing the pH, none of these chelating sets are capable of preventing the hydrolysis of the metal ion. The formation of stable complexes was found in the nickel(II) and copper(II) systems above pH ∼ 6 with a [NH2, Namide, Nhydrox.] binding mode after deprotonation and coordination of the peptide amide and the hydroxamate group. With an excess of copper(II), the formation of trinuclear [Cu3HxL2]x+4 type (x = -4 to -6) complexes as the major species was also detected. Blocking the terminal amino group in the Z-protected ligands results in a dramatic decrease of the nickel(II) and zinc(II) binding strengths, and insoluble complexes with copper(II). No indication was found for the role of the hydroxyl group of the serine moiety in metal ion binding.

Original languageEnglish
Pages (from-to)1625-1633
Number of pages9
JournalPolyhedron
Volume26
Issue number8
DOIs
Publication statusPublished - May 21 2007

Fingerprint

Hydroxamic Acids
Dipeptides
Coordination Complexes
Metal complexes
Peptides
peptides
Metal ions
Copper
metal ions
Nickel
Metals
Ions
aqueous solutions
Derivatives
Zinc
acids
Acids
copper
Aluminum
metals

Keywords

  • Equilibrium
  • Metal complex
  • Micro constant
  • Peptide hydroxamic acid
  • pH-potentiometry
  • Stability constant

ASJC Scopus subject areas

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

Cite this

New insights into the metal ion-peptide hydroxamate interactions : Metal complexes of primary hydroxamic acid derivatives of common dipeptides in aqueous solution. / Buglyó, P.; Nagy, Eszter Márta; Farkas, E.; Sóvágó, I.; Sanna, Daniele; Micera, Giovanni.

In: Polyhedron, Vol. 26, No. 8, 21.05.2007, p. 1625-1633.

Research output: Contribution to journalArticle

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abstract = "Complex formation of primary dipeptide hydroxamic acids, L-Ala-L-AlaNHOH and L-Ala-L-SerNHOH, as well as the corresponding Z-protected ones, Z-L-Ala-L-AlaNHOH and Z-L-Ala-L-SerNHOH (Z = benzyloxycarbonyl), with iron(III), aluminium(III), nickel(II), copper(II) and zinc(II) was studied in aqueous solution by pH-potentiometric and spectroscopic (UV-Vis, EPR, CD, 1H NMR) methods. The exclusive formation of [O,O] chelated hydroxamate complexes was found with iron(III) and aluminium(III) with all the ligands. Formation of linkage isomers with the involvement of either [O,O] hydroxamate or [NH2,CO] chelates was detected both in the zinc(II)-L-Ala-L-AlaNHOH and -L-Ala-L-SerNHOH systems. Upon increasing the pH, none of these chelating sets are capable of preventing the hydrolysis of the metal ion. The formation of stable complexes was found in the nickel(II) and copper(II) systems above pH ∼ 6 with a [NH2, Namide, Nhydrox.] binding mode after deprotonation and coordination of the peptide amide and the hydroxamate group. With an excess of copper(II), the formation of trinuclear [Cu3HxL2]x+4 type (x = -4 to -6) complexes as the major species was also detected. Blocking the terminal amino group in the Z-protected ligands results in a dramatic decrease of the nickel(II) and zinc(II) binding strengths, and insoluble complexes with copper(II). No indication was found for the role of the hydroxyl group of the serine moiety in metal ion binding.",
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T2 - Metal complexes of primary hydroxamic acid derivatives of common dipeptides in aqueous solution

AU - Buglyó, P.

AU - Nagy, Eszter Márta

AU - Farkas, E.

AU - Sóvágó, I.

AU - Sanna, Daniele

AU - Micera, Giovanni

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N2 - Complex formation of primary dipeptide hydroxamic acids, L-Ala-L-AlaNHOH and L-Ala-L-SerNHOH, as well as the corresponding Z-protected ones, Z-L-Ala-L-AlaNHOH and Z-L-Ala-L-SerNHOH (Z = benzyloxycarbonyl), with iron(III), aluminium(III), nickel(II), copper(II) and zinc(II) was studied in aqueous solution by pH-potentiometric and spectroscopic (UV-Vis, EPR, CD, 1H NMR) methods. The exclusive formation of [O,O] chelated hydroxamate complexes was found with iron(III) and aluminium(III) with all the ligands. Formation of linkage isomers with the involvement of either [O,O] hydroxamate or [NH2,CO] chelates was detected both in the zinc(II)-L-Ala-L-AlaNHOH and -L-Ala-L-SerNHOH systems. Upon increasing the pH, none of these chelating sets are capable of preventing the hydrolysis of the metal ion. The formation of stable complexes was found in the nickel(II) and copper(II) systems above pH ∼ 6 with a [NH2, Namide, Nhydrox.] binding mode after deprotonation and coordination of the peptide amide and the hydroxamate group. With an excess of copper(II), the formation of trinuclear [Cu3HxL2]x+4 type (x = -4 to -6) complexes as the major species was also detected. Blocking the terminal amino group in the Z-protected ligands results in a dramatic decrease of the nickel(II) and zinc(II) binding strengths, and insoluble complexes with copper(II). No indication was found for the role of the hydroxyl group of the serine moiety in metal ion binding.

AB - Complex formation of primary dipeptide hydroxamic acids, L-Ala-L-AlaNHOH and L-Ala-L-SerNHOH, as well as the corresponding Z-protected ones, Z-L-Ala-L-AlaNHOH and Z-L-Ala-L-SerNHOH (Z = benzyloxycarbonyl), with iron(III), aluminium(III), nickel(II), copper(II) and zinc(II) was studied in aqueous solution by pH-potentiometric and spectroscopic (UV-Vis, EPR, CD, 1H NMR) methods. The exclusive formation of [O,O] chelated hydroxamate complexes was found with iron(III) and aluminium(III) with all the ligands. Formation of linkage isomers with the involvement of either [O,O] hydroxamate or [NH2,CO] chelates was detected both in the zinc(II)-L-Ala-L-AlaNHOH and -L-Ala-L-SerNHOH systems. Upon increasing the pH, none of these chelating sets are capable of preventing the hydrolysis of the metal ion. The formation of stable complexes was found in the nickel(II) and copper(II) systems above pH ∼ 6 with a [NH2, Namide, Nhydrox.] binding mode after deprotonation and coordination of the peptide amide and the hydroxamate group. With an excess of copper(II), the formation of trinuclear [Cu3HxL2]x+4 type (x = -4 to -6) complexes as the major species was also detected. Blocking the terminal amino group in the Z-protected ligands results in a dramatic decrease of the nickel(II) and zinc(II) binding strengths, and insoluble complexes with copper(II). No indication was found for the role of the hydroxyl group of the serine moiety in metal ion binding.

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KW - pH-potentiometry

KW - Stability constant

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