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The Inhibition of Amyloid Fibrillation Using the Proteolytic Products of PQQ-Modified α-Synuclein

The inhibition of amyloid fibril and/or oligomer formation allows a novel therapeutic approach to neurodegen- erative diseases such as Parkinson's disease. We have previously reported that pyrroloquinoline quinone (PQQ), a cofac- tor in the bacterial oxidative metabolism of alcohols, prevents the amyloid formation of � -synuclein, which is the causa- tive 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.