Citation: ZHANG Bao-Hong, HU Guo-Sheng, ZHU Deng-Sen, WANG Wen-Ji, GONG Ge-Hui, DU Wei-Hong. Inhibition of Prion Amyloid Peptide Fibril Formation by Peroxovanadium Complexes[J]. Acta Physico-Chimica Sinica, ;2016, 32(7): 1810-1818. doi: 10.3866/PKU.WHXB201604145 shu

Inhibition of Prion Amyloid Peptide Fibril Formation by Peroxovanadium Complexes

1.
College of Materials Science and Engineering, North University of China, Taiyuan 030051, P. R. China;
2.
Department of Chemistry, Renmin University of China, Beijing 100872, P. R. China

Received Date: 29 February 2016
Revised Date: 11 April 2016

Fund Project: The project was supported by the National Natural Science Foundation of China (21271185, 21473251).

Interactions of peroxovanadiumcomplexes (NH₄)[VO(O₂)₂(bipy)]·4H₂O (1) and (NH₄)[VO(O₂)₂(phen)]· 2H₂O (2) with the mutant peptide M109F of prion neuropeptide PrP106-126 have been investigated by fluorescence spectroscopy (FS), nuclear magnetic resonance (NMR), electron spray ionization mass spectrometry (ESI-MS) and transmission electron microscopy (TEM) methods. The results show that the peroxovanadium complexes may directly bind to the M109F peptide, and react with the peptide by methionine oxidation at Met112, resulting in the inhibition of M109F peptide aggregation. Compared with complex 2, complex 1 shows improved inhibitory effects on peptide M109F. Both complexes 1 and 2 exhibit an increased cellular viability against amyloid peptide-induced cytotoxicity. The basic data for the investigation of potential metallodrugs against neurodegenerative disease are provided.
- Prion neuropeptide,
- Peroxovanadium complex,
- Fibril formation,
- Methionine oxidation,
- Cytotoxicity
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1.
沈阳化工大学材料科学与工程学院沈阳 110142