A study of the reactions of a methionine- and histidine-containing tetrapeptide with different Pd(ii) and Pt(ii) complexes: Selective cleavage of the amide bond by platination of the peptide and steric modification of the catalyst

Sneana Rajković, Marija D. Ivković, C. Kállay, I. Sóvágó, Milo I. Djuran

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Abstract

1H NMR spectroscopy was applied to the study of the reactions of [M(en)(H2O)2]2+ complexes (M = Pd(ii) and Pt(ii)) with the N-acetylated methionyl-glycyl-histidyl-glycineamide, MeCOMet-Gly-His-GlyNH2. All reactions were performed in the pH range 1.5-2.0 with equimolar amounts of the [M(en)(H2O)2] 2+ complex and the tetrapeptide at 60°C. In all these reactions, a metal(ii) complex bound to a methionine residue affects the regioselective cleavage of the amide bond involving the carboxylic group of methionine. The priority in the cleavage of the Met-Gly amide bond in relation to the other amide bonds in this peptide is due to the high affinity of Pt(ii) and Pd(ii) ions for the sulfur donor atom. The mechanism of these hydrolytic reactions is discussed and, for its clarification, the reaction of the [Pd(en)(H 2O)2]2+ complex with MeCOMet-Gly-His-GlyNH 2 was additionally investigated by potentiometric titration. The steric effects of the various palladium(ii) complexes of the type [Pd(L)(H 2O)2]2+, in which L is a chelating diamine (ethylenediamine, en, 2-picolylamine, pic, or 2,2-dipyridylamine, dpa) on the hydrolytic cleavage of the amide bond involving the carboxylic group of histidine in the MeCOMet-Gly-His-GlyNH2 tetrapeptide were also studied by 1H NMR spectroscopy. All reactions were performed under the above-mentioned conditions and in the initial stage of these reactions, the MeCOMet-Gly-His-GlyNH2 was reacted with an equimolar amount of the [Pt(dien)Cl]+ complex (dien is diethylenetriamine) and then the monoplatinated [Pt(dien)(MeCOMet-Gly-His-GlyNH2-S)]2+ complex was treated with an equimolar amount of [Pd(L)(H2O) 2]2+. It was found that the rate of hydrolysis of the His-GlyNH2 amide bond in [Pt(dien)(MeCOMet-Gly-His-GlyNH 2-S)]2+ decreased from the en to the pic complex, with finally a total inhibition of this reaction with [Pd(dpa)(H2O) 2]2+. These results are an important step in the study of the regioselective cleavage of peptides and proteins and in the development of new palladium(ii) complexes as artificial metallopeptidases.

Original languageEnglish
Pages (from-to)8370-8377
Number of pages8
JournalDalton Transactions
Issue number39
DOIs
Publication statusPublished - 2009

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Histidine
Amides
Methionine
Peptides
Catalysts
ethylenediamine
Palladium
Nuclear magnetic resonance spectroscopy
Diamines
Metalloproteases
Metal complexes
Chelation
Titration
Sulfur
Hydrolysis
Ions
Atoms
diaquadiethylenediamineplatinum(II)
Proteins

ASJC Scopus subject areas

  • Inorganic Chemistry

Cite this

@article{b0c864325c6f4867a5137e8f5031d24a,
title = "A study of the reactions of a methionine- and histidine-containing tetrapeptide with different Pd(ii) and Pt(ii) complexes: Selective cleavage of the amide bond by platination of the peptide and steric modification of the catalyst",
abstract = "1H NMR spectroscopy was applied to the study of the reactions of [M(en)(H2O)2]2+ complexes (M = Pd(ii) and Pt(ii)) with the N-acetylated methionyl-glycyl-histidyl-glycineamide, MeCOMet-Gly-His-GlyNH2. All reactions were performed in the pH range 1.5-2.0 with equimolar amounts of the [M(en)(H2O)2] 2+ complex and the tetrapeptide at 60°C. In all these reactions, a metal(ii) complex bound to a methionine residue affects the regioselective cleavage of the amide bond involving the carboxylic group of methionine. The priority in the cleavage of the Met-Gly amide bond in relation to the other amide bonds in this peptide is due to the high affinity of Pt(ii) and Pd(ii) ions for the sulfur donor atom. The mechanism of these hydrolytic reactions is discussed and, for its clarification, the reaction of the [Pd(en)(H 2O)2]2+ complex with MeCOMet-Gly-His-GlyNH 2 was additionally investigated by potentiometric titration. The steric effects of the various palladium(ii) complexes of the type [Pd(L)(H 2O)2]2+, in which L is a chelating diamine (ethylenediamine, en, 2-picolylamine, pic, or 2,2-dipyridylamine, dpa) on the hydrolytic cleavage of the amide bond involving the carboxylic group of histidine in the MeCOMet-Gly-His-GlyNH2 tetrapeptide were also studied by 1H NMR spectroscopy. All reactions were performed under the above-mentioned conditions and in the initial stage of these reactions, the MeCOMet-Gly-His-GlyNH2 was reacted with an equimolar amount of the [Pt(dien)Cl]+ complex (dien is diethylenetriamine) and then the monoplatinated [Pt(dien)(MeCOMet-Gly-His-GlyNH2-S)]2+ complex was treated with an equimolar amount of [Pd(L)(H2O) 2]2+. It was found that the rate of hydrolysis of the His-GlyNH2 amide bond in [Pt(dien)(MeCOMet-Gly-His-GlyNH 2-S)]2+ decreased from the en to the pic complex, with finally a total inhibition of this reaction with [Pd(dpa)(H2O) 2]2+. These results are an important step in the study of the regioselective cleavage of peptides and proteins and in the development of new palladium(ii) complexes as artificial metallopeptidases.",
author = "Sneana Rajković and Ivković, {Marija D.} and C. K{\'a}llay and I. S{\'o}v{\'a}g{\'o} and Djuran, {Milo I.}",
year = "2009",
doi = "10.1039/b908182h",
language = "English",
pages = "8370--8377",
journal = "Dalton Transactions",
issn = "1477-9226",
publisher = "Royal Society of Chemistry",
number = "39",

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TY - JOUR

T1 - A study of the reactions of a methionine- and histidine-containing tetrapeptide with different Pd(ii) and Pt(ii) complexes

T2 - Selective cleavage of the amide bond by platination of the peptide and steric modification of the catalyst

AU - Rajković, Sneana

AU - Ivković, Marija D.

AU - Kállay, C.

AU - Sóvágó, I.

AU - Djuran, Milo I.

PY - 2009

Y1 - 2009

N2 - 1H NMR spectroscopy was applied to the study of the reactions of [M(en)(H2O)2]2+ complexes (M = Pd(ii) and Pt(ii)) with the N-acetylated methionyl-glycyl-histidyl-glycineamide, MeCOMet-Gly-His-GlyNH2. All reactions were performed in the pH range 1.5-2.0 with equimolar amounts of the [M(en)(H2O)2] 2+ complex and the tetrapeptide at 60°C. In all these reactions, a metal(ii) complex bound to a methionine residue affects the regioselective cleavage of the amide bond involving the carboxylic group of methionine. The priority in the cleavage of the Met-Gly amide bond in relation to the other amide bonds in this peptide is due to the high affinity of Pt(ii) and Pd(ii) ions for the sulfur donor atom. The mechanism of these hydrolytic reactions is discussed and, for its clarification, the reaction of the [Pd(en)(H 2O)2]2+ complex with MeCOMet-Gly-His-GlyNH 2 was additionally investigated by potentiometric titration. The steric effects of the various palladium(ii) complexes of the type [Pd(L)(H 2O)2]2+, in which L is a chelating diamine (ethylenediamine, en, 2-picolylamine, pic, or 2,2-dipyridylamine, dpa) on the hydrolytic cleavage of the amide bond involving the carboxylic group of histidine in the MeCOMet-Gly-His-GlyNH2 tetrapeptide were also studied by 1H NMR spectroscopy. All reactions were performed under the above-mentioned conditions and in the initial stage of these reactions, the MeCOMet-Gly-His-GlyNH2 was reacted with an equimolar amount of the [Pt(dien)Cl]+ complex (dien is diethylenetriamine) and then the monoplatinated [Pt(dien)(MeCOMet-Gly-His-GlyNH2-S)]2+ complex was treated with an equimolar amount of [Pd(L)(H2O) 2]2+. It was found that the rate of hydrolysis of the His-GlyNH2 amide bond in [Pt(dien)(MeCOMet-Gly-His-GlyNH 2-S)]2+ decreased from the en to the pic complex, with finally a total inhibition of this reaction with [Pd(dpa)(H2O) 2]2+. These results are an important step in the study of the regioselective cleavage of peptides and proteins and in the development of new palladium(ii) complexes as artificial metallopeptidases.

AB - 1H NMR spectroscopy was applied to the study of the reactions of [M(en)(H2O)2]2+ complexes (M = Pd(ii) and Pt(ii)) with the N-acetylated methionyl-glycyl-histidyl-glycineamide, MeCOMet-Gly-His-GlyNH2. All reactions were performed in the pH range 1.5-2.0 with equimolar amounts of the [M(en)(H2O)2] 2+ complex and the tetrapeptide at 60°C. In all these reactions, a metal(ii) complex bound to a methionine residue affects the regioselective cleavage of the amide bond involving the carboxylic group of methionine. The priority in the cleavage of the Met-Gly amide bond in relation to the other amide bonds in this peptide is due to the high affinity of Pt(ii) and Pd(ii) ions for the sulfur donor atom. The mechanism of these hydrolytic reactions is discussed and, for its clarification, the reaction of the [Pd(en)(H 2O)2]2+ complex with MeCOMet-Gly-His-GlyNH 2 was additionally investigated by potentiometric titration. The steric effects of the various palladium(ii) complexes of the type [Pd(L)(H 2O)2]2+, in which L is a chelating diamine (ethylenediamine, en, 2-picolylamine, pic, or 2,2-dipyridylamine, dpa) on the hydrolytic cleavage of the amide bond involving the carboxylic group of histidine in the MeCOMet-Gly-His-GlyNH2 tetrapeptide were also studied by 1H NMR spectroscopy. All reactions were performed under the above-mentioned conditions and in the initial stage of these reactions, the MeCOMet-Gly-His-GlyNH2 was reacted with an equimolar amount of the [Pt(dien)Cl]+ complex (dien is diethylenetriamine) and then the monoplatinated [Pt(dien)(MeCOMet-Gly-His-GlyNH2-S)]2+ complex was treated with an equimolar amount of [Pd(L)(H2O) 2]2+. It was found that the rate of hydrolysis of the His-GlyNH2 amide bond in [Pt(dien)(MeCOMet-Gly-His-GlyNH 2-S)]2+ decreased from the en to the pic complex, with finally a total inhibition of this reaction with [Pd(dpa)(H2O) 2]2+. These results are an important step in the study of the regioselective cleavage of peptides and proteins and in the development of new palladium(ii) complexes as artificial metallopeptidases.

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