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Short Communication

Pyrroloquinoline quinone inhibits the fibrillation of amyloid proteins

Jihoon Kim, Masaki Kobayashi, Makoto Fukuda, Daisuke Ogasawara, Natsuki Kobayashi, Sungwoong Han, Chikashi Nakamura, Masaki Inada, Chisato Miyaura, Kazunori Ikebukuro and Koji Sode

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 β (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 β (1-42) also decreased. With further advanced pharmacological approaches, PQQ may become a leading anti-neurodegenerative compound in the treatment of neurodegenerative diseases.

Authors

Jihoon Kim

Tokyo University of Agriculture & Technology

Masaki Kobayashi

Tokyo University of Agriculture & Technology

Makoto Fukuda

Tokyo University of Agriculture & Technology

Daisuke Ogasawara

Tokyo University of Agriculture & Technology

Natsuki Kobayashi

Tokyo University of Agriculture & Technology

Sungwoong Han

Tokyo University of Agriculture & Technology; National Institute of Advanced Industrial Science & Technology

Chikashi Nakamura

Tokyo University of Agriculture & Technology; National Institute of Advanced Industrial Science & Technology

Masaki Inada

Tokyo University of Agriculture & Technology

Chisato Miyaura

Tokyo University of Agriculture & Technology

Kazunori Ikebukuro

Tokyo University of Agriculture & Technology

Koji Sode Corresponding author: sode@cc.tuat.ac.jp

Tokyo University of Agriculture & Technology