Pyrroloquinoline quinone inhibits the fibrillation of amyloid proteins

被引:35
作者
Kim, Jihoon [1 ]
Kobayashi, Masaki [1 ]
Fukuda, Makoto [1 ]
Ogasawara, Daisuke [1 ]
Kobayashi, Natsuki [1 ]
Han, Sungwoong [1 ,3 ]
Nakamura, Chikashi [1 ,3 ]
Inada, Masaki [1 ]
Miyaura, Chisato [1 ]
Ikebukuro, Kazunori [1 ]
Sode, Koji [1 ,2 ]
机构
[1] Tokyo Univ Agr & Technol, Dept Biotechnol, Grad Sch Engn, Koganei, Tokyo 184, Japan
[2] Tokyo Univ Agr & Technol, Dept Technol Risk Management, Grad Sch Technol Management, Koganei, Tokyo 184, Japan
[3] Natl Inst Adv Ind Sci & Technol, Res Inst Cell Engn, Koto Ku, Tokyo, Japan
关键词
amyloid beta; amyloid fibril; cytotoxicity; fibril formation; inhibitor; prion; pyrroloquinoline quinone; MAMMALIAN PRION PROTEIN; IN-VITRO CONVERSION; ALPHA-SYNUCLEIN; ALZHEIMERS-DISEASE; WILD-TYPE; AGGREGATION; FIBRILS; NEURODEGENERATION; MECHANISM; CYTOTOXICITY;
D O I
10.4161/pri.4.1.10889
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
Several neurodegenerative diseases involve the selective damage of neuron cells resulting from the accumulation of amyloid fibril formation. Considering that the formation of amyloid fibrils as well as their precursor oligomers is cytotoxic, the agents that prevent the formation of oligomers and/or fibrils might allow the development of a novel therapeutic approach to neurodegenerative diseases. Here, we show pyrroloquinoline quinone (PQQ) inhibits the amyloid fibril formation of the amyloid proteins, amyloid beta (1-42) and mouse prion protein. The fibril formation of mouse prion protein in the presence of PQQ was dramatically prevented. Similarly, the fibril formation of amyloid beta (1-42) also decreased. With further advanced pharmacological approaches, PQQ may become a leading anti-neurodegenerative compound in the treatment of neurodegenerative diseases.
引用
收藏
页码:26 / 31
页数:6
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