Al(III)-binding ability of an octapeptide and its phosphorylated derivative

Dominik Hollender, Andrea Károly-Lakatos, P. Forgó, T. Körtvélyesi, G. Dombi, Zs. Majer, M. Hollósi, T. Kiss, Akira Odani

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

A synthetic octapeptide, H-GlyGluGlyGluGlySerGlyGly-OH, and its phosphorylated Ser derivative were synthetized and their solution speciation and binding modes in their complexes with Al(III) were measured. One goal of the work was find a lead compound for the design of a selective peptide-based Al(III) chelator. pH-potentiometry was used to characterize the stoichiometry and the stability of the species formed in the interactions of the metal ion and the peptides, while multinuclear NMR was applied to characterize the binding sites of the metal ion in the complexes. CD spectroscopy revealed a difference in the conformational behaviour of the phosphorylated peptide as compared with its non-phosphorylated parent derivative. The Al(III) is presumed to enhance aggregation through the -PO3H - Al3+-PO32 - Al3+- intermolecular bindings between the peptide chains. The results of molecular dynamics calculations supported the experimentally obtained secondary structures and the binding position of Al(III).

Original languageEnglish
Pages (from-to)351-361
Number of pages11
JournalJournal of Inorganic Biochemistry
Volume100
Issue number3
DOIs
Publication statusPublished - Mar 2006

Fingerprint

Derivatives
Peptides
Metal ions
Metals
Potentiometry
Ions
Biomolecular Nuclear Magnetic Resonance
Lead compounds
Molecular Dynamics Simulation
Chelating Agents
Stoichiometry
Molecular dynamics
Spectrum Analysis
Agglomeration
Binding Sites
Nuclear magnetic resonance
Spectroscopy
Lead

Keywords

  • MD calculations
  • Neurodegeneration
  • NMR
  • Speciation

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry

Cite this

Al(III)-binding ability of an octapeptide and its phosphorylated derivative. / Hollender, Dominik; Károly-Lakatos, Andrea; Forgó, P.; Körtvélyesi, T.; Dombi, G.; Majer, Zs.; Hollósi, M.; Kiss, T.; Odani, Akira.

In: Journal of Inorganic Biochemistry, Vol. 100, No. 3, 03.2006, p. 351-361.

Research output: Contribution to journalArticle

@article{58710c558ca0401fb413a670d550d956,
title = "Al(III)-binding ability of an octapeptide and its phosphorylated derivative",
abstract = "A synthetic octapeptide, H-GlyGluGlyGluGlySerGlyGly-OH, and its phosphorylated Ser derivative were synthetized and their solution speciation and binding modes in their complexes with Al(III) were measured. One goal of the work was find a lead compound for the design of a selective peptide-based Al(III) chelator. pH-potentiometry was used to characterize the stoichiometry and the stability of the species formed in the interactions of the metal ion and the peptides, while multinuclear NMR was applied to characterize the binding sites of the metal ion in the complexes. CD spectroscopy revealed a difference in the conformational behaviour of the phosphorylated peptide as compared with its non-phosphorylated parent derivative. The Al(III) is presumed to enhance aggregation through the -PO3H - Al3+-PO32 - Al3+- intermolecular bindings between the peptide chains. The results of molecular dynamics calculations supported the experimentally obtained secondary structures and the binding position of Al(III).",
keywords = "MD calculations, Neurodegeneration, NMR, Speciation",
author = "Dominik Hollender and Andrea K{\'a}roly-Lakatos and P. Forg{\'o} and T. K{\"o}rtv{\'e}lyesi and G. Dombi and Zs. Majer and M. Holl{\'o}si and T. Kiss and Akira Odani",
year = "2006",
month = "3",
doi = "10.1016/j.jinorgbio.2005.11.023",
language = "English",
volume = "100",
pages = "351--361",
journal = "Journal of Inorganic Biochemistry",
issn = "0162-0134",
publisher = "Elsevier Inc.",
number = "3",

}

TY - JOUR

T1 - Al(III)-binding ability of an octapeptide and its phosphorylated derivative

AU - Hollender, Dominik

AU - Károly-Lakatos, Andrea

AU - Forgó, P.

AU - Körtvélyesi, T.

AU - Dombi, G.

AU - Majer, Zs.

AU - Hollósi, M.

AU - Kiss, T.

AU - Odani, Akira

PY - 2006/3

Y1 - 2006/3

N2 - A synthetic octapeptide, H-GlyGluGlyGluGlySerGlyGly-OH, and its phosphorylated Ser derivative were synthetized and their solution speciation and binding modes in their complexes with Al(III) were measured. One goal of the work was find a lead compound for the design of a selective peptide-based Al(III) chelator. pH-potentiometry was used to characterize the stoichiometry and the stability of the species formed in the interactions of the metal ion and the peptides, while multinuclear NMR was applied to characterize the binding sites of the metal ion in the complexes. CD spectroscopy revealed a difference in the conformational behaviour of the phosphorylated peptide as compared with its non-phosphorylated parent derivative. The Al(III) is presumed to enhance aggregation through the -PO3H - Al3+-PO32 - Al3+- intermolecular bindings between the peptide chains. The results of molecular dynamics calculations supported the experimentally obtained secondary structures and the binding position of Al(III).

AB - A synthetic octapeptide, H-GlyGluGlyGluGlySerGlyGly-OH, and its phosphorylated Ser derivative were synthetized and their solution speciation and binding modes in their complexes with Al(III) were measured. One goal of the work was find a lead compound for the design of a selective peptide-based Al(III) chelator. pH-potentiometry was used to characterize the stoichiometry and the stability of the species formed in the interactions of the metal ion and the peptides, while multinuclear NMR was applied to characterize the binding sites of the metal ion in the complexes. CD spectroscopy revealed a difference in the conformational behaviour of the phosphorylated peptide as compared with its non-phosphorylated parent derivative. The Al(III) is presumed to enhance aggregation through the -PO3H - Al3+-PO32 - Al3+- intermolecular bindings between the peptide chains. The results of molecular dynamics calculations supported the experimentally obtained secondary structures and the binding position of Al(III).

KW - MD calculations

KW - Neurodegeneration

KW - NMR

KW - Speciation

UR - http://www.scopus.com/inward/record.url?scp=33244471100&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33244471100&partnerID=8YFLogxK

U2 - 10.1016/j.jinorgbio.2005.11.023

DO - 10.1016/j.jinorgbio.2005.11.023

M3 - Article

VL - 100

SP - 351

EP - 361

JO - Journal of Inorganic Biochemistry

JF - Journal of Inorganic Biochemistry

SN - 0162-0134

IS - 3

ER -