Interaction studies of oxindole-derivatives with β-amyloid peptides inhibiting its aggregation induced by metal ions
Some hydrazones and Schiff bases derived from isatin, an endogenous oxindole formed in the metabolism of tryptophan, were obtained to investigate their effects on in vitro aggregation of β-amyloid peptides (Aβ), macromolecules implicated in Alzheimer's disease. Some hydrazone ligands, prepared...
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Published in | Journal of inorganic biochemistry Vol. 245; p. 112227 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
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Elsevier Inc
01.08.2023
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Abstract | Some hydrazones and Schiff bases derived from isatin, an endogenous oxindole formed in the metabolism of tryptophan, were obtained to investigate their effects on in vitro aggregation of β-amyloid peptides (Aβ), macromolecules implicated in Alzheimer's disease. Some hydrazone ligands, prepared by condensation reactions of isatin with hydrazine derivatives, showed a large affinity binding to the synthetic peptides Aβ, particularly to Aβ1–16. Measurements by NMR spectroscopy indicated that those interactions occur mainly at the metal binding site of the peptide, involving His6, His13, and His14 residues, and that hydrazone E-diastereoisomer interacts preferentially with the amyloid peptides. Experimental results were consistent with simulations using a docking approach, where it is demonstrated that the amino acid residues Glu3, His6, His13, and His14 are those that mostly interact with the ligands. Further, these oxindole-derived ligands can efficiently chelate copper(II) and zinc(II) ions, forming moderate stable [ML] 1:1 species. The corresponding formation constants were determined by UV/Vis spectroscopy, by titrations of the ligands with increasing amounts of metal salts, and the obtained log K values were in the range 2.74 to 5.11. Both properties, good affinity for amyloid peptides, and reasonably good capacity of chelating biometal ions, like copper and zinc, can explain the efficient inhibition of Aβ fragments aggregation, as shown by experiments carried out with the oxindole derivatives in the presence of metal ions.
Synopsis: Some hydrazones and Schiff bases derived from an endogenous oxindole were obtained, and investigated about their effects on in vitro aggregation of β-amyloid peptides (Aβ), implicated in Alzheimer's disease. [Display omitted]
•Schiff base and hydrazine-derivatives of isatin were synthesized.•These ligands form stable copper and zinc complexes characterized spectroscopically.•Strong interactions of a hydrazine-derivative with amyloid peptide were verified.•Interactions occur mainly through histine residues, involving E-diastereoisomer.•Noteworthy peptide aggregation inhibition was shown in the presence of such ligands. |
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AbstractList | Some hydrazones and Schiff bases derived from isatin, an endogenous oxindole formed in the metabolism of tryptophan, were obtained to investigate their effects on in vitro aggregation of β-amyloid peptides (Aβ), macromolecules implicated in Alzheimer's disease. Some hydrazone ligands, prepared by condensation reactions of isatin with hydrazine derivatives, showed a large affinity binding to the synthetic peptides Aβ, particularly to Aβ
. Measurements by NMR spectroscopy indicated that those interactions occur mainly at the metal binding site of the peptide, involving His6, His13, and His14 residues, and that hydrazone E-diastereoisomer interacts preferentially with the amyloid peptides. Experimental results were consistent with simulations using a docking approach, where it is demonstrated that the amino acid residues Glu3, His6, His13, and His14 are those that mostly interact with the ligands. Further, these oxindole-derived ligands can efficiently chelate copper(II) and zinc(II) ions, forming moderate stable [ML] 1:1 species. The corresponding formation constants were determined by UV/Vis spectroscopy, by titrations of the ligands with increasing amounts of metal salts, and the obtained log K values were in the range 2.74 to 5.11. Both properties, good affinity for amyloid peptides, and reasonably good capacity of chelating biometal ions, like copper and zinc, can explain the efficient inhibition of Aβ fragments aggregation, as shown by experiments carried out with the oxindole derivatives in the presence of metal ions. Some hydrazones and Schiff bases derived from isatin, an endogenous oxindole formed in the metabolism of tryptophan, were obtained to investigate their effects on in vitro aggregation of β-amyloid peptides (Aβ), macromolecules implicated in Alzheimer's disease. Some hydrazone ligands, prepared by condensation reactions of isatin with hydrazine derivatives, showed a large affinity binding to the synthetic peptides Aβ, particularly to Aβ1–16. Measurements by NMR spectroscopy indicated that those interactions occur mainly at the metal binding site of the peptide, involving His6, His13, and His14 residues, and that hydrazone E-diastereoisomer interacts preferentially with the amyloid peptides. Experimental results were consistent with simulations using a docking approach, where it is demonstrated that the amino acid residues Glu3, His6, His13, and His14 are those that mostly interact with the ligands. Further, these oxindole-derived ligands can efficiently chelate copper(II) and zinc(II) ions, forming moderate stable [ML] 1:1 species. The corresponding formation constants were determined by UV/Vis spectroscopy, by titrations of the ligands with increasing amounts of metal salts, and the obtained log K values were in the range 2.74 to 5.11. Both properties, good affinity for amyloid peptides, and reasonably good capacity of chelating biometal ions, like copper and zinc, can explain the efficient inhibition of Aβ fragments aggregation, as shown by experiments carried out with the oxindole derivatives in the presence of metal ions. Synopsis: Some hydrazones and Schiff bases derived from an endogenous oxindole were obtained, and investigated about their effects on in vitro aggregation of β-amyloid peptides (Aβ), implicated in Alzheimer's disease. [Display omitted] •Schiff base and hydrazine-derivatives of isatin were synthesized.•These ligands form stable copper and zinc complexes characterized spectroscopically.•Strong interactions of a hydrazine-derivative with amyloid peptide were verified.•Interactions occur mainly through histine residues, involving E-diastereoisomer.•Noteworthy peptide aggregation inhibition was shown in the presence of such ligands. |
ArticleNumber | 112227 |
Author | Machini, M. Teresa Casella, Luigi Novato, Willian Tássio Gomes Pirota, Valentina Monzani, Enrico Costa, Luiz Antônio Sodré Wegermann, Camila Anchau da Costa Ferreira, Ana Maria |
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Keywords | PBS AChE AD DMSO Oxindole-derived hydrazones Oxindolimines MeCN isapn Peptide aggregation inhibition PDB Aβ DFT isahpy misapn HEPES Binding constants IC50 ROS Amyloid peptides isahim Metal complexes |
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SubjectTerms | Alzheimer Disease - metabolism Amyloid beta-Peptides - chemistry Amyloid peptides Binding constants Copper - chemistry Humans Ions Isatin Ligands Metal complexes Metals Oxindole-derived hydrazones Oxindoles Oxindolimines Peptide aggregation inhibition Peptide Fragments - chemistry Zinc - chemistry |
Title | Interaction studies of oxindole-derivatives with β-amyloid peptides inhibiting its aggregation induced by metal ions |
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