Platinum(II) , Complexes Inhibit the Aggregation of Amyloid Model Systems

Overview

Journal Int J Mol Sci

Publisher MDPI

Specialties Biochemistry
Chemistry
Molecular Biology

Date 2019 Feb 17

PMID 30769904

Citations 10

Authors

Daniele Florio

Anna Maria Malfitano

Sarah Di Somma

Carolin Mugge

Wolfgang Weigand

Giarita Ferraro

Ilaria Iacobucci

Maria Monti

Giancarlo Morelli

Antonello Merlino

Daniela Marasco

Affiliations

Soon will be listed here.

Abstract

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 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.

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