Complexes of aluminium with peptide ligands: A fourier transform IR spectroscopic study

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Abstract

Aluminium has been recognized to be a neurotoxic agent and a risk factor in Alzheimer's disease and other neuronal dysfunctions. CD spectroscopic studies on two synthetic fragments of the human neurofilament protein midsized subunit (NF-M), and their alanine-for-serine-substituted and/or serine-phosphorylated derivatives showed the formation of stable, citric acid resistant complexes of Al3+ with peptide ligands [M. Hollosi, Z. M. Shen, A. Perczel, and G. D. Fasman (1994) Proc. Natl. Acad. Sci. USA, vol. 9, pp. 4902-4906]. In the case of Ser-phosphorylated fragments, a β-sheet inducing effect of Ca2+ and Al3+ ions was observed. However, the serine-containing parent peptides. NF-M13 (KSPVPKSPVEEKG) and NF-M17 (EEKGKSPVPKSPVEEKG), failed to show CD spectral changes reflecting β-sheet formation upon addition of Al3+ ions. On the basis of the amide 1 region of the Fourier transform ir spectra, in trifluoroethanol, the peptide backbone of NF-M17 and NF-M17 (A6A11) shows marked changes in the presence of Al3+. The most significant spectral differences are seen in the carboxyl region (> 1700 cm- 1). The high-frequency component bands above 1760 cm-1 in both spectra belong to the C=O of undissociated CF3COOH. Another strong band at 1710 cm- 1, which appears only in the spectrum of NF-M17 (A6 A11) (NF-M17 with Ser6 and Ser11 replaced by Ala) can be assigned to the side chain or C- terminal COOH groups. The differential protonation state of the carboxyl groups in the two peptides suggests the formation of Al3+ complexes of different structure and stability. The Al3+ complex of NF-M17 (A6 A11) is likely less stable, or one or more of the carboxylates are not coordinated to the Al3+ and thus can serve as a base to bind the liberated protons. In NF-M17 the OH groups of serines facilitate the formation of type [Al · pep(H-1)] complexes with the involvement of all carboxylate groups in the molecule. The relevance of intramolecular and intermolecular Al3+ binding to the controversial biological role of aluminium is also discussed.

Original languageEnglish
Pages (from-to)381-389
Number of pages9
JournalBiopolymers - Peptide Science Section
Volume36
Issue number3
DOIs
Publication statusPublished - 1995

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Fourier Analysis
Aluminum
Serine
Peptides
Fourier transforms
Ligands
Ions
Trifluoroethanol
Protonation
Citric acid
Protein Subunits
Amides
Citric Acid
Alanine
Protons
Alzheimer Disease
Derivatives
Proteins
Molecules

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics

Cite this

@article{c4bb5f539e774d7e87a1ebea623d6540,
title = "Complexes of aluminium with peptide ligands: A fourier transform IR spectroscopic study",
abstract = "Aluminium has been recognized to be a neurotoxic agent and a risk factor in Alzheimer's disease and other neuronal dysfunctions. CD spectroscopic studies on two synthetic fragments of the human neurofilament protein midsized subunit (NF-M), and their alanine-for-serine-substituted and/or serine-phosphorylated derivatives showed the formation of stable, citric acid resistant complexes of Al3+ with peptide ligands [M. Hollosi, Z. M. Shen, A. Perczel, and G. D. Fasman (1994) Proc. Natl. Acad. Sci. USA, vol. 9, pp. 4902-4906]. In the case of Ser-phosphorylated fragments, a β-sheet inducing effect of Ca2+ and Al3+ ions was observed. However, the serine-containing parent peptides. NF-M13 (KSPVPKSPVEEKG) and NF-M17 (EEKGKSPVPKSPVEEKG), failed to show CD spectral changes reflecting β-sheet formation upon addition of Al3+ ions. On the basis of the amide 1 region of the Fourier transform ir spectra, in trifluoroethanol, the peptide backbone of NF-M17 and NF-M17 (A6A11) shows marked changes in the presence of Al3+. The most significant spectral differences are seen in the carboxyl region (> 1700 cm- 1). The high-frequency component bands above 1760 cm-1 in both spectra belong to the C=O of undissociated CF3COOH. Another strong band at 1710 cm- 1, which appears only in the spectrum of NF-M17 (A6 A11) (NF-M17 with Ser6 and Ser11 replaced by Ala) can be assigned to the side chain or C- terminal COOH groups. The differential protonation state of the carboxyl groups in the two peptides suggests the formation of Al3+ complexes of different structure and stability. The Al3+ complex of NF-M17 (A6 A11) is likely less stable, or one or more of the carboxylates are not coordinated to the Al3+ and thus can serve as a base to bind the liberated protons. In NF-M17 the OH groups of serines facilitate the formation of type [Al · pep(H-1)] complexes with the involvement of all carboxylate groups in the molecule. The relevance of intramolecular and intermolecular Al3+ binding to the controversial biological role of aluminium is also discussed.",
author = "M. Holl{\'o}si and S. Holly and Zs. Majer and I. Laczk{\'o} and Fasman, {G. D.}",
year = "1995",
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pages = "381--389",
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TY - JOUR

T1 - Complexes of aluminium with peptide ligands

T2 - A fourier transform IR spectroscopic study

AU - Hollósi, M.

AU - Holly, S.

AU - Majer, Zs.

AU - Laczkó, I.

AU - Fasman, G. D.

PY - 1995

Y1 - 1995

N2 - Aluminium has been recognized to be a neurotoxic agent and a risk factor in Alzheimer's disease and other neuronal dysfunctions. CD spectroscopic studies on two synthetic fragments of the human neurofilament protein midsized subunit (NF-M), and their alanine-for-serine-substituted and/or serine-phosphorylated derivatives showed the formation of stable, citric acid resistant complexes of Al3+ with peptide ligands [M. Hollosi, Z. M. Shen, A. Perczel, and G. D. Fasman (1994) Proc. Natl. Acad. Sci. USA, vol. 9, pp. 4902-4906]. In the case of Ser-phosphorylated fragments, a β-sheet inducing effect of Ca2+ and Al3+ ions was observed. However, the serine-containing parent peptides. NF-M13 (KSPVPKSPVEEKG) and NF-M17 (EEKGKSPVPKSPVEEKG), failed to show CD spectral changes reflecting β-sheet formation upon addition of Al3+ ions. On the basis of the amide 1 region of the Fourier transform ir spectra, in trifluoroethanol, the peptide backbone of NF-M17 and NF-M17 (A6A11) shows marked changes in the presence of Al3+. The most significant spectral differences are seen in the carboxyl region (> 1700 cm- 1). The high-frequency component bands above 1760 cm-1 in both spectra belong to the C=O of undissociated CF3COOH. Another strong band at 1710 cm- 1, which appears only in the spectrum of NF-M17 (A6 A11) (NF-M17 with Ser6 and Ser11 replaced by Ala) can be assigned to the side chain or C- terminal COOH groups. The differential protonation state of the carboxyl groups in the two peptides suggests the formation of Al3+ complexes of different structure and stability. The Al3+ complex of NF-M17 (A6 A11) is likely less stable, or one or more of the carboxylates are not coordinated to the Al3+ and thus can serve as a base to bind the liberated protons. In NF-M17 the OH groups of serines facilitate the formation of type [Al · pep(H-1)] complexes with the involvement of all carboxylate groups in the molecule. The relevance of intramolecular and intermolecular Al3+ binding to the controversial biological role of aluminium is also discussed.

AB - Aluminium has been recognized to be a neurotoxic agent and a risk factor in Alzheimer's disease and other neuronal dysfunctions. CD spectroscopic studies on two synthetic fragments of the human neurofilament protein midsized subunit (NF-M), and their alanine-for-serine-substituted and/or serine-phosphorylated derivatives showed the formation of stable, citric acid resistant complexes of Al3+ with peptide ligands [M. Hollosi, Z. M. Shen, A. Perczel, and G. D. Fasman (1994) Proc. Natl. Acad. Sci. USA, vol. 9, pp. 4902-4906]. In the case of Ser-phosphorylated fragments, a β-sheet inducing effect of Ca2+ and Al3+ ions was observed. However, the serine-containing parent peptides. NF-M13 (KSPVPKSPVEEKG) and NF-M17 (EEKGKSPVPKSPVEEKG), failed to show CD spectral changes reflecting β-sheet formation upon addition of Al3+ ions. On the basis of the amide 1 region of the Fourier transform ir spectra, in trifluoroethanol, the peptide backbone of NF-M17 and NF-M17 (A6A11) shows marked changes in the presence of Al3+. The most significant spectral differences are seen in the carboxyl region (> 1700 cm- 1). The high-frequency component bands above 1760 cm-1 in both spectra belong to the C=O of undissociated CF3COOH. Another strong band at 1710 cm- 1, which appears only in the spectrum of NF-M17 (A6 A11) (NF-M17 with Ser6 and Ser11 replaced by Ala) can be assigned to the side chain or C- terminal COOH groups. The differential protonation state of the carboxyl groups in the two peptides suggests the formation of Al3+ complexes of different structure and stability. The Al3+ complex of NF-M17 (A6 A11) is likely less stable, or one or more of the carboxylates are not coordinated to the Al3+ and thus can serve as a base to bind the liberated protons. In NF-M17 the OH groups of serines facilitate the formation of type [Al · pep(H-1)] complexes with the involvement of all carboxylate groups in the molecule. The relevance of intramolecular and intermolecular Al3+ binding to the controversial biological role of aluminium is also discussed.

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