The binding of Cu(II) by the peptide with β-Asp located in non-coordinating site - Solution and structural studies

A. Janicka-Klos; H. Czapor-Irzabek; Z. Czyznikowska; M. Cebrat; J. Brasun

doi:10.1016/j.ica.2014.05.017

The binding of Cu(II) by the peptide with β-Asp located in non-coordinating site - Solution and structural studies

A. Janicka-Klos, H. Czapor-Irzabek, Z. Czyznikowska, M. Cebrat, J. Brasun

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

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Abstract

In the present study, the coordination abilities of Ac- TLEGTKKGHKLHLβDY-NH₂ peptide (the analogue of SPARC 114-128 fragment containing β-Asp¹²⁷ residue) are discussed. The analysis is provided based on the results of potentiometric and spectroscopic measurements supported by quantum-chemical calculations. Presented results clearly show that the β-Asp amino acid residue may influence the efficiency of metal ion binding despite the fact that it is not directly involved in metal ion binding. Moreover, in order to further characterize experimentally observed species, we performed quantum-chemical calculations for structures mimicking SPARC 114-128 fragment as a step towards a better understanding of structural and energetical aspects related to the coordination abilities of the analogue of SPARC fragment.

Original language	English (US)
Pages (from-to)	67-73
Number of pages	7
Journal	Inorganica Chimica Acta
Volume	421
DOIs	https://doi.org/10.1016/j.ica.2014.05.017
State	Published - Sep 1 2014
Externally published	Yes

Keywords

Copper(II) complexes
SPARC
β-Asp
β-Peptides

ASJC Scopus subject areas

Inorganic Chemistry
Physical and Theoretical Chemistry
Materials Chemistry

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10.1016/j.ica.2014.05.017

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title = "The binding of Cu(II) by the peptide with β-Asp located in non-coordinating site - Solution and structural studies",

abstract = "In the present study, the coordination abilities of Ac- TLEGTKKGHKLHLβDY-NH2 peptide (the analogue of SPARC 114-128 fragment containing β-Asp127 residue) are discussed. The analysis is provided based on the results of potentiometric and spectroscopic measurements supported by quantum-chemical calculations. Presented results clearly show that the β-Asp amino acid residue may influence the efficiency of metal ion binding despite the fact that it is not directly involved in metal ion binding. Moreover, in order to further characterize experimentally observed species, we performed quantum-chemical calculations for structures mimicking SPARC 114-128 fragment as a step towards a better understanding of structural and energetical aspects related to the coordination abilities of the analogue of SPARC fragment.",

keywords = "Copper(II) complexes, SPARC, β-Asp, β-Peptides",

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T1 - The binding of Cu(II) by the peptide with β-Asp located in non-coordinating site - Solution and structural studies

AU - Janicka-Klos, A.

AU - Czapor-Irzabek, H.

AU - Czyznikowska, Z.

AU - Cebrat, M.

AU - Brasun, J.

PY - 2014/9/1

Y1 - 2014/9/1

N2 - In the present study, the coordination abilities of Ac- TLEGTKKGHKLHLβDY-NH2 peptide (the analogue of SPARC 114-128 fragment containing β-Asp127 residue) are discussed. The analysis is provided based on the results of potentiometric and spectroscopic measurements supported by quantum-chemical calculations. Presented results clearly show that the β-Asp amino acid residue may influence the efficiency of metal ion binding despite the fact that it is not directly involved in metal ion binding. Moreover, in order to further characterize experimentally observed species, we performed quantum-chemical calculations for structures mimicking SPARC 114-128 fragment as a step towards a better understanding of structural and energetical aspects related to the coordination abilities of the analogue of SPARC fragment.

AB - In the present study, the coordination abilities of Ac- TLEGTKKGHKLHLβDY-NH2 peptide (the analogue of SPARC 114-128 fragment containing β-Asp127 residue) are discussed. The analysis is provided based on the results of potentiometric and spectroscopic measurements supported by quantum-chemical calculations. Presented results clearly show that the β-Asp amino acid residue may influence the efficiency of metal ion binding despite the fact that it is not directly involved in metal ion binding. Moreover, in order to further characterize experimentally observed species, we performed quantum-chemical calculations for structures mimicking SPARC 114-128 fragment as a step towards a better understanding of structural and energetical aspects related to the coordination abilities of the analogue of SPARC fragment.

KW - Copper(II) complexes

KW - SPARC

KW - β-Asp

KW - β-Peptides

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JO - Inorganica Chimica Acta

JF - Inorganica Chimica Acta

ER -

The binding of Cu(II) by the peptide with β-Asp located in non-coordinating site - Solution and structural studies

Abstract

Keywords

ASJC Scopus subject areas

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