Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 20, Issue 4, Pages -Publisher
MDPI
DOI: 10.3390/ijms20040829
Keywords
amyloid aggregation; platinum complexes; anti-aggregation properties
Funding
- University of Naples Federico II [000005 ALTRI_DR_409_2017_Rec_Ateneo_prof_MARASCO]
- POR CAMPANIA FESR 2014/2020 PROGETTO PREMIO INFRASTRUTTURA PER LA MEDICINA DI PRECISIONE IN ONCOLOGIA
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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 A, 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 IC50 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 -hydroxy dithiocinnamic esters can be used to develop platinum or platinoid compounds with anti-amyloid aggregation properties.
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