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BMC Bioinformatics

, 8:451

First Online: 16 November 2007Received: 26 July 2007Accepted: 16 November 2007


Backgroundα-Synuclein is a Parkinson-s-disease-related protein. It forms aggregates in vivo, and these aggregates cause cell cytotoxicity. Aggregation inhibitors are expected to reduce α-synuclein cytotoxicity, and an aggregation accelerator has recently been reported to reduce α-synuclein cytotoxicity. Therefore, amyloid aggregation modulating ligands are expected to serve as therapeutic medicines.

ResultsWe screened peptide ligands against α-synuclein by in silico panning, a method which we have proposed previously. In this study, we selected as the target a very hydrophobic region known as the amyloid-core-forming region. Since this region cannot be dissolved in water, it is difficult to carry out the in vitro screening of its peptide ligand. We carried out 6 rounds of in silico panning using a genetic algorithm and a docking simulation. After the in silico panning, we evaluated the top peptides screened in silico by in vitro assay. These peptides were capable of binding to α-synuclein.

ConclusionWe demonstrated that it is possible to screen α-synuclein-binding peptides by in silico panning. The screened peptides bind to α-synuclein, thus affecting the aggregation of α-synuclein.

Electronic supplementary materialThe online version of this article doi:10.1186-1471-2105-8-451 contains supplementary material, which is available to authorized users.

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Autor: Koichi Abe - Natsuki Kobayashi - Koji Sode - Kazunori Ikebukuro


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