Platinum(II) <em>O</em>,<em>S</em> Complexes Inhibit the Aggregation of Amyloid Model Systems

Platinum(II) <em>O</em>,<em>S</em> Complexes Inhibit the Aggregation of Amyloid Model Systems

Platinum(II) complexes with different cinnamic acid derivatives as ligands were investigated for their ability to inhibit the aggregation process of amyloid systems derived from Aβ, Yeast Prion Protein Sup35p and the C-terminal domain of nucleophosmin 1. Thioflavin T binding assays and circular dich...

Full description

Bibliographic Details
Main Authors: Daniele Florio, Anna Maria Malfitano, Sarah Di Somma, Carolin Mügge, Wolfgang Weigand, Giarita Ferraro, Ilaria Iacobucci, Maria Monti, Giancarlo Morelli, Antonello Merlino, Daniela Marasco
Format: Article
Language:English
Published: MDPI AG 2019-02-01
Series:International Journal of Molecular Sciences
Subjects:
amyloid aggregation
platinum complexes
anti-aggregation properties
Online Access:https://www.mdpi.com/1422-0067/20/4/829
Description
Summary:Platinum(II) complexes with different cinnamic acid derivatives as ligands were investigated for their ability to inhibit the aggregation process of amyloid systems derived from Aβ, Yeast Prion Protein Sup35p and the C-terminal domain of nucleophosmin 1. Thioflavin T binding assays and circular dichroism data indicate that these compounds strongly inhibit the aggregation of investigated peptides exhibiting IC<sub>50</sub> values in the micromolar range. MS analysis confirms the formation of adducts between peptides and Pt(II) complexes that are also able to reduce amyloid cytotoxicity in human SH-SY5Y neuroblastoma cells. Overall data suggests that bidentate ligands based on β-hydroxy dithiocinnamic esters can be used to develop platinum or platinoid compounds with anti-amyloid aggregation properties.
ISSN:1422-0067

Similar Items