Chemical Synthesis of Alpha‐Synuclein Proteins via Solid‐Phase Peptide Synthesis and Native Chemical Ligation
2023-04-27 | journal article. A publication with affiliation to the University of Göttingen.
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Chemical Synthesis of Alpha‐Synuclein Proteins via Solid‐Phase Peptide Synthesis and Native Chemical Ligation
Gatzemeier, L. M.; Meyer, F.; Diederichsen, U. & Outeiro, T. F. (2023)
Chemistry: a European Journal, 29(33) art. e202300649. DOI: https://doi.org/10.1002/chem.202300649
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Details
- Authors
- Gatzemeier, Luisa Maria; Meyer, Franc; Diederichsen, Ulf; Outeiro, Tiago Fleming
- Abstract
- Alpha-Synuclein (α-Synuclein) is a 140 amino acid protein implicated in neurodegenerative disorders known as synucleinopathies, where it accumulates in proteinaceous inclusions in the brain. The normal physiological function of α-Synuclein remains obscure, as it exists in several non-neuronal cells in which its function has not been studied. Given the tremendous interest in studying α-Synuclein, and the existing limitations in the production of modified forms of the protein, we developed a method for the chemical synthesis of α-Synuclein by combining peptide fragment synthesis via automated microwave-assisted solid-phase peptide synthesis and ligation strategies. Our synthetic pathway enables the synthesis of protein variants of interest, carrying either mutations or posttranslational modifications, for further investigations of the effects on the structure and aggregation behavior of the protein. Ultimately, our study forms the foundation for future syntheses and studies of other custom-made α-Synuclein variants with a single or several modifications, as necessary.
- Issue Date
- 27-April-2023
- Journal
- Chemistry: a European Journal
- Project
- SFB 1286: Quantitative Synaptologie
SFB 1286 | B08: Definition von Kaskaden molekularer Veränderungen bei Synucleinopathien während der Neurodegeneration
EXC 2067: Multiscale Bioimaging - Working Group
- RG Outeiro (Experimental Neurodegeneration)
- ISSN
- 0947-6539; 1521-3765
- eISSN
- 1521-3765
- Language
- English
- Sponsor
- Deutsche Forschungsgemeinschaft http://dx.doi.org/10.13039/501100001659
University of Göttingen http://dx.doi.org/10.13039/501100003385