A Comparative Study of the Effects of Platinum (II) Complexes on β-Amyloid Aggregation: Potential Neurodrug Applications

Herein the effects of three platinum complexes, namely ( -4-2)-(2,2'-bipyridine)dichloridoplatinum(II), Pt-bpy, ( -4-2)-dichlorido(1,10-phenanthroline) platinum(II), Pt-phen, and ( -4-2)-chlorido(2,2':6',2''-terpyridine)platinum(II) chloride, Pt-terpy, on the aggregation of...

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Veröffentlicht in:International journal of molecular sciences 2021-03, Vol.22 (6), p.3015
Hauptverfasser: Manna, Sara La, Florio, Daniele, Iacobucci, Ilaria, Napolitano, Fabiana, Benedictis, Ilaria De, Malfitano, Anna Maria, Monti, Maria, Ravera, Mauro, Gabano, Elisabetta, Marasco, Daniela
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container_issue 6
container_start_page 3015
container_title International journal of molecular sciences
container_volume 22
creator Manna, Sara La
Florio, Daniele
Iacobucci, Ilaria
Napolitano, Fabiana
Benedictis, Ilaria De
Malfitano, Anna Maria
Monti, Maria
Ravera, Mauro
Gabano, Elisabetta
Marasco, Daniela
description Herein the effects of three platinum complexes, namely ( -4-2)-(2,2'-bipyridine)dichloridoplatinum(II), Pt-bpy, ( -4-2)-dichlorido(1,10-phenanthroline) platinum(II), Pt-phen, and ( -4-2)-chlorido(2,2':6',2''-terpyridine)platinum(II) chloride, Pt-terpy, on the aggregation of an amyloid model system derived from the C-terminal domain of Aβ peptide (Aβ ) were investigated. Thioflavin T (ThT) binding assays revealed the ability of Pt(II) compounds to repress amyloid aggregation in a dose-dependent way, whereas the ability of Aβ peptide to interfere with ligand field of metal complexes was analyzed through UV-Vis absorption spectroscopy and electrospray ionization mass spectrometry. Spectroscopic data provided micromolar EC values and allowed to assess that the observed inhibition of amyloid aggregation is due to the formation of adducts between Aβ peptide and complexes upon the release of labile ligands as chloride and that they can explore different modes of coordination toward Aβ with respect to the entire Aβ polypeptide. In addition, conformational studies through circular dichroism (CD) spectroscopy suggested that Pt-terpy induces soluble β-structures of monomeric Aβ , thus limiting self-recognition. Noticeably, Pt-terpy demonstrated the ability to reduce the cytotoxicity of amyloid peptide in human SH-SY5Y neuroblastoma cells. Presented data corroborate the hypothesis to enlarge the application field of already known metal-based agents to neurodegenerative diseases, as potential neurodrugs.
doi_str_mv 10.3390/ijms22063015
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source MDPI - Multidisciplinary Digital Publishing Institute; MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central
subjects Absorption spectroscopy
Adducts
Alzheimer's disease
Amino Acid Sequence
Amyloid beta-Peptides - chemistry
Benzothiazoles - metabolism
Cell Death - drug effects
Cell Line, Tumor
Cell Proliferation - drug effects
Chloride
Chlorides
Circular dichroism
Comparative studies
Cytotoxicity
Dichroism
Fluorescence
Humans
Investigations
Ligands
Mass spectrometry
Mass spectroscopy
Neuroblasts
Peptide Fragments - chemistry
Peptides
Platinum
Platinum - chemistry
Platinum - pharmacology
Polypeptides
Protein Aggregates - drug effects
Protein Stability
Scientific imaging
Self-recognition
Solubility
Spectrophotometry, Ultraviolet
Time Factors
β-Amyloid
title A Comparative Study of the Effects of Platinum (II) Complexes on β-Amyloid Aggregation: Potential Neurodrug Applications
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