Methionine Oxidation in Human Prion Protein – Design of Anti- and 
Pro-Aggregation Variants

Wolschner, Christina

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Thesis

Methionine Oxidation in Human Prion Protein – Design of Anti- and Pro-Aggregation Variants

MPS-Authors

/persons/resource/persons78905

Wolschner, Christina
Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society;

External Resource

No external resources are shared

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

Wolschner, C. (2009). Methionine Oxidation in Human Prion Protein – Design of Anti- and Pro-Aggregation Variants. PhD Thesis, Technische Universität, München.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0010-59A6-C

Abstract

The aim of this thesis was to examine the pathological relevance of the oxidation state of methionine (Met) side chains in neurodegenerative disorders such as sporadic prion disease. First for better understanding the oxidative event, the effect and consequences of Met oxidation in the recombinant human cellular prion protein (rhPrPC23-231) were studied. Second the incorporation of stable Met analogs, norleucine and methoxinine, in rhPrPC23-231 mimicking the reduced and oxidized state of Met, respectively – was performed. The results strongly indicate a correlation of the α → β secondary structure conversion in rhPrPC with the oxidative state of the Met residues. In the future, this approach will certainly be useful for studying diseases, which arise from protein misfolding due to oxidative stress