Peptides as Modulators of α-Synuclein Aggregation

Author(s): Paolo Ruzza, Matteo Gazziero, Maria De Marchi, Giada Massalongo, Anna Marchiani, Ida Autiero, Isabella Tessari, Luigi Bubacco, Andrea Cald

Journal Name: Protein & Peptide Letters

Volume 22 , Issue 4 , 2015

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Graphical Abstract:


α-Synuclein forms amyloid deposits in the dopaminergic neurons; a process that is believed to contribute to the Parkinson’s disease. An emerging theme in amyloid research is the hypothesis that the toxic species produced during amyloid formation share common physic-chemical features and exert their effects by common modes. This prompted the idea that molecules able to inhibit a protein aggregation process may cross-react with other amyloidogenic proteins, interfering in their fibrils formation. We investigate the ability of analogues of the heptapeptide H-Arg-Lys-Val-MePhe-Tyr-Thr-Trp- OH2, an inhibitor of Aβ-peptide aggregation, to cross-react with α-synuclein interfering with its fibril formation. The influence of the MePhe topography on the interaction with α-synuclein has also been evaluated, replacing the MePhe residue with either Phe or the conformationally restricted Tic residues. Peptides interact with good affinity with the

Keywords: α-synuclein, β-breaker peptides, conformational constraints, protein-peptide interaction.

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Article Details

Year: 2015
Page: [354 - 361]
Pages: 8
DOI: 10.2174/0929866522666150209142649
Price: $65

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