Pyrroloquinoline quinone inhibits the fibrillation of amyloid proteins.
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.
Kim
Jihoon
J
Department of Biotechnology, Graduate School of Engineering, Tokyo University of Agriculture & Technology, Koganei-shi, Tokyo, Japan.
Kobayashi
Masaki
M
Fukuda
Makoto
M
Ogasawara
Daisuke
D
Kobayashi
Natsuki
N
Han
Sungwoong
S
Nakamura
Chikashi
C
Inada
Masaki
M
Miyaura
Chisato
C
Ikebukuro
Kazunori
K
Sode
Koji
K
D000682:Amyloid / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D006801:Humans; D051379:Mice; D015394:Molecular Structure; D019636:Neurodegenerative Diseases / Q000188:drug therapy; D045542:PQQ Cofactor / Q000737:chemistry / Q000494:pharmacology* / Q000627:therapeutic use
D000682:Amyloid; D045542:PQQ Cofactor