The Inhibition of Amyloid Fibrillation Using the Proteolytic Products of PQQ-Modified ..-Synuclein
- نوع فایل : کتاب
- زبان : انگلیسی
- مؤلف : Natsuki Kobayashi1, Jihoon Kim1, Kazunori Ikebukuro1 and Koji Sode1,2,*
- چاپ و سال / کشور: 2009
Description
The inhibition of amyloid fibril and/or oligomer formation allows a novel therapeutic approach to neurodegenerative diseases such as Parkinson’s disease. We have previously reported that pyrroloquinoline quinone (PQQ), a cofactor in the bacterial oxidative metabolism of alcohols, prevents the amyloid formation of ..-synuclein, which is the causative factor of Parkinson’s disease. Moreover, PQQ-modified ..-synuclein is also able to inhibit the fibrillation of intact ..- synuclein. Here, we demonstrate that PQQ-modified peptide fragments, the proteolytic products of PQQ-modified ..- synuclein, prevent the amyloid formation of full-length ..-synuclein, and that these inhibitory effects are derived from the PQQ modification of the peptide. Moreover, these effects are likely to be peptide-sequence-dependent. Thus, the specific interaction between the full-length ..-synuclein and the peptide region of the PQQ-modified peptide prevents amyloid formation.
The Open Biotechnology Journal, 2009, 3, 40-45
