NDLI: Roles of DMSO-type ruthenium complexes in disaggregation of prion neuropeptide PrP106

Content Provider	Royal Society of Chemistry (RSC)
Author	Zhu, Dengsen Wang, Baohuai Wang, Xuesong Zhao, Cong Wang, Wenji Du, Weihong
Copyright Year	2016
Abstract	Ruthenium complexes are potential anticancer metallodrugs and inhibitors of various proteins, such as enzymes and even amyloid peptides. Studies on Aβ protein, human islet amyloid polypeptide, and prion neuropeptide have indicated that Ru complexes can inhibit amyloidosis. However, the interaction mechanism of peptides with Ru complexes remains unclear. In this study, we selected four dimethyl sulfoxide (DMSO)-type Ru complexes containing large aromatic ligands to explore and compare the interactions of Ru complexes with the prion neuropeptide PrP106–126. Results showed that, unlike new anti-tumor metastasis inhibitor-A-like compounds, these complexes can bind to PrP106–126 mainly through metal coordination and hydrophobic interaction. The Ru complexes disaggregated the PrP106–126 fibrils into scattered fragments or amorphous forms, thereby reducing the toxicity of PrP106–126. Among the four Ru complexes, complex 1, which consists of bipyridyl and DMSO ligands, exhibited the highest disaggregation ability and relatively high cell viability, which may be attributed to its molecular configuration and low cytotoxicity. These results suggested that Ru complexes are promising metallodrugs against amyloidosis-related diseases.
Starting Page	16055
Ending Page	16065
Page Count	11
File Format	HTM / HTML PDF
ISSN	20462069
Volume Number	6
Issue Number	19
Journal	RSC Advances
DOI	10.1039/c5ra21523d
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Ruthenium DMSO Amylin Dimethyl sulfoxide Cytotoxicity Amyloid Prion Amyloidosis Metastasis Hydrophobe Neuropeptide Protein
Content Type	Text
Resource Type	Article
Subject	Chemistry Chemical Engineering

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