| Autor: |
Giada Massalongo, Maria De Marchi, Matteo Gazziero, Ida Autiero, Paolo Ruzza, Isabella Tessari, Anna Marchiani, Luigi Bubacco, Andrea Calderan |
| Rok vydání: |
2015 |
| Předmět: |
|
| Zdroj: |
Protein & Peptide Letters. 22:354-361 |
| ISSN: |
0929-8665 |
| DOI: |
10.2174/0929866522666150209142649 |
| Popis: |
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 α-synuclein monomer, promoting its aggregation process. This work provides the basis for the development of new drugs based on peptidomimetics able to modify the oligomers - mature fibrils equilibrium towards this last species. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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