This title appears in the Scientific Report :
2008
Please use the identifier:
http://dx.doi.org/10.1089/rej.2008.0698 in citations.
Aggregation and amyloid fibril formation of the prion protein is accelerated in presence of glycogen
Aggregation and amyloid fibril formation of the prion protein is accelerated in presence of glycogen
Prion diseases like Creutzfeldt-Jakob disease in humans or scrapie in sheep and goats are infectious neurodegenerative diseases. Their infectious agent, called prion, is composed mainly of aggregated and misfolded prion protein and non-proteinaceous components. An example of such a common non-protei...
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Personal Name(s): | Panza, G. |
---|---|
Stöhr, J. / Birkmann, E. / Riesner, D. / Willbold, D. / Baba, O. / Terashima, T. / Dumpitak, C. | |
Contributing Institute: |
Molekulare Biophysik; INB-2 |
Published in: | Rejuvenation research, 11 (2008) S. 365 - 369 |
Imprint: |
Larchmont, NY
Liebert
2008
|
Physical Description: |
365 - 369 |
PubMed ID: |
18341429 |
DOI: |
10.1089/rej.2008.0698 |
Document Type: |
Journal Article |
Research Program: |
Funktion und Dysfunktion des Nervensystems |
Series Title: |
Rejuvenation Research
11 |
Subject (ZB): | |
Publikationsportal JuSER |
Prion diseases like Creutzfeldt-Jakob disease in humans or scrapie in sheep and goats are infectious neurodegenerative diseases. Their infectious agent, called prion, is composed mainly of aggregated and misfolded prion protein and non-proteinaceous components. An example of such a common non-proteinaceous secondary component of natural prions is the polysaccharide scaffold. We studied the influence of such a polysaccharide on the conformational transition of PrP applying an in vitro conversion system. Here we report that glycogen supports and accelerates PrP amorphous aggregation similar to seeded aggregation and leads to co-aggregates. Furthermore, PrP fibril formation was highly accelerated in the presence of glycogen. |