Acta Phys. -Chim. Sin. ›› 2016, Vol. 32 ›› Issue (7): 1810-1818.doi: 10.3866/PKU.WHXB201604145

• ARTICLE • Previous Articles     Next Articles

Inhibition of Prion Amyloid Peptide Fibril Formation by Peroxovanadium Complexes

Bao-Hong ZHANG1,2,Guo-Sheng HU1,*(),Deng-Sen ZHU2,Wen-Ji WANG2,Ge-Hui GONG2,Wei-Hong DU2,*()   

  1. 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:2016-02-29 Published:2016-07-08
  • Contact: Guo-Sheng HU,Wei-Hong DU E-mail:chinahugsh@hotmail.com;whdu@ruc.edu.cn
  • Supported by:
    the National Natural Science Foundation of China(21271185);National Natural Science Foundation of China(21473251)

Abstract:

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.

Key words: Prion neuropeptide, Peroxovanadium complex, Fibril formation, Methionine oxidation, Cytotoxicity

MSC2000: 

  • O641