The role of the βasp residue in copper(II) binding by modified peptides

Hanna Czapor-Irzabek; Marek Cebrat; Justyna Brasuń

doi:10.1016/j.tetlet.2012.01.087

The role of the βasp residue in copper(II) binding by modified peptides

Hanna Czapor-Irzabek, Marek Cebrat, Justyna Brasuń

Research output: Contribution to journal › Article › peer-review

1 Scopus citations

Abstract

The synthesis and binding abilities of peptides containing β-amino acids towards Cu(II) ions are presented. The peptides studied were: Ala-βAsp-Ser-Gly and Arg-Lys-βAsp-Val-Tyr. Potentiometric titrations were carried out to establish the stoichiometry of the resulting metal-ligand complexes. The copper(II) coordination mode of the complexes was investigated by performing detailed spectroscopic analyses (UV-Vis, CD) in strict correlation with potentiometric measurements. The results obtained on the β-peptides studied allowed the characterization of the influence of this structural modification on the coordination abilities of the peptides. Moreover, the role of the α-Asp position in the peptide chain was also described.

Original language	English (US)
Pages (from-to)	1652-1655
Number of pages	4
Journal	Tetrahedron Letters
Volume	53
Issue number	13
DOIs	https://doi.org/10.1016/j.tetlet.2012.01.087
State	Published - Mar 28 2012
Externally published	Yes

Keywords

β-Amino acid
β-Peptide
Complex
Copper(II)

ASJC Scopus subject areas

Biochemistry
Organic Chemistry
Drug Discovery

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10.1016/j.tetlet.2012.01.087

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title = "The role of the βasp residue in copper(II) binding by modified peptides",

abstract = "The synthesis and binding abilities of peptides containing β-amino acids towards Cu(II) ions are presented. The peptides studied were: Ala-βAsp-Ser-Gly and Arg-Lys-βAsp-Val-Tyr. Potentiometric titrations were carried out to establish the stoichiometry of the resulting metal-ligand complexes. The copper(II) coordination mode of the complexes was investigated by performing detailed spectroscopic analyses (UV-Vis, CD) in strict correlation with potentiometric measurements. The results obtained on the β-peptides studied allowed the characterization of the influence of this structural modification on the coordination abilities of the peptides. Moreover, the role of the α-Asp position in the peptide chain was also described.",

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T1 - The role of the βasp residue in copper(II) binding by modified peptides

AU - Czapor-Irzabek, Hanna

AU - Cebrat, Marek

AU - Brasuń, Justyna

PY - 2012/3/28

Y1 - 2012/3/28

N2 - The synthesis and binding abilities of peptides containing β-amino acids towards Cu(II) ions are presented. The peptides studied were: Ala-βAsp-Ser-Gly and Arg-Lys-βAsp-Val-Tyr. Potentiometric titrations were carried out to establish the stoichiometry of the resulting metal-ligand complexes. The copper(II) coordination mode of the complexes was investigated by performing detailed spectroscopic analyses (UV-Vis, CD) in strict correlation with potentiometric measurements. The results obtained on the β-peptides studied allowed the characterization of the influence of this structural modification on the coordination abilities of the peptides. Moreover, the role of the α-Asp position in the peptide chain was also described.

AB - The synthesis and binding abilities of peptides containing β-amino acids towards Cu(II) ions are presented. The peptides studied were: Ala-βAsp-Ser-Gly and Arg-Lys-βAsp-Val-Tyr. Potentiometric titrations were carried out to establish the stoichiometry of the resulting metal-ligand complexes. The copper(II) coordination mode of the complexes was investigated by performing detailed spectroscopic analyses (UV-Vis, CD) in strict correlation with potentiometric measurements. The results obtained on the β-peptides studied allowed the characterization of the influence of this structural modification on the coordination abilities of the peptides. Moreover, the role of the α-Asp position in the peptide chain was also described.

KW - β-Amino acid

KW - β-Peptide

KW - Complex

KW - Copper(II)

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JO - Tetrahedron Letters

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ER -

The role of the βasp residue in copper(II) binding by modified peptides

Abstract

Keywords

ASJC Scopus subject areas

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