Peptides as Modulators of α-Synuclein Aggregation

Title:Peptides as Modulators of α-Synuclein Aggregation

Volume: 22 Issue: 4

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

Affiliation:

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

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

Cite this article as:

Ruzza Paolo, Gazziero Matteo, De Marchi Maria, Massalongo Giada, Marchiani Anna, Autiero Ida, Tessari Isabella, Bubacco Luigi and Cald Andrea, Peptides as Modulators of α-Synuclein Aggregation, Protein & Peptide Letters 2015; 22 (4) . https://dx.doi.org/10.2174/0929866522666150209142649