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

被引：40

作者：

Florio, Daniele ^{[1
]}

Malfitano, Anna Maria ^{[2
]}

Di Somma, Sarah ^{[2
]}

Muegge, Carolin ^{[3
,4
]}

Weigand, Wolfgang ^{[3
]}

Ferraro, Giarita ^{[5
]}

Iacobucci, Ilaria ^{[5
,6
]}

Monti, Maria ^{[5
,6
]}

Morelli, Giancarlo ^{[1
]}

Merlino, Antonello ^{[5
]}

Marasco, Daniela ^{[1
]}

机构：

[1] Univ Naples Federico II, Dept Pharm, I-80134 Naples, Italy

[2] Univ Naples Federico II, Dept Translat Med Sci, I-80131 Naples, Italy

[3] Univ Jena, Inst Inorgan & Analyt Chem, D-07743 Jena, Germany

[4] Ruhr Univ Bochum, Dept Biol, D-44801 Bochum, Germany

[5] Univ Naples Federico II, Dept Chem Sci, I-80126 Naples, Italy

[6] Univ Naples Federico II, CEINGE Biotecnol Avanzate Scarl, I-80145 Naples, Italy

来源：

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES | 2019年 / 20卷 / 04期

关键词：

amyloid aggregation; platinum complexes; anti-aggregation properties; BETA PEPTIDE; RUTHENIUM COMPLEXES; CISPLATIN BINDING; FIBRIL FORMATION; IN-VITRO; PROTEINS; MODULATION; DRUGS; IDENTIFICATION; IRIDIUM(III);

D O I：

10.3390/ijms20040829

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页数：13

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