Publication Details

Category Text Publication
Reference Category Journals
DOI 10.1016/j.jmb.2009.07.014
Title (Primary) Peptide NMHRYPNQ of the Cellular Prion Protein (PrPC) Inhibits Aggregation and Is a Potential Key for Understanding Prion-Prion Interactions
Author Rehders, D.; Classen, B.; Redecke, L.; Buschke, A.; Reibe, C.; Jehmlich, N. ORCID logo ; von Bergen, M.; Betzel, A.; Meyer, B.
Source Titel Journal of Molecular Biology
Year 2009
Department METABOX; PROTEOM
Volume 392
Issue 1
Page From 198
Page To 207
Language englisch
Keywords Surface plasmon resonance; BSE; aggregation; NMR binding epitope
Abstract Pathogenesis of transmissible spongiform encephalopathies is correlated with a conversion of the normal cellular form of the prion protein (PrPC) into the abnormal isoform (scrapie form of PrP). Contact of the normal PrP with its abnormal isoform, the scrapie form of PrP, induces the transformation. Knowledge of molecules that inhibit such contacts leads to an understanding of the mechanism of the aggregation, and these molecules may serve as leads for drugs against transmissible spongiform encephalopathies. Therefore, we screened a synthetic octapeptide library of the globular domain of the human PrPC for binding affinity to PrPC. Two fragments with binding affinity, 149YYRENMHR156 and 153NMHRYPNQ160, were identified with Kd values of 21 and 25 µM, respectively. A 10-fold excess of peptide 153NMHRYPNQ160 inhibits aggregation of the PrP by 99%. NMR and mass spectrometry showed that the binding region of the peptide 153NMHRYPNQ160 is located at helix 3 of the PrP.
Persistent UFZ Identifier https://www.ufz.de/index.php?en=20939&ufzPublicationIdentifier=515
Rehders, D., Classen, B., Redecke, L., Buschke, A., Reibe, C., Jehmlich, N., von Bergen, M., Betzel, A., Meyer, B. (2009):
Peptide NMHRYPNQ of the Cellular Prion Protein (PrPC) Inhibits Aggregation and Is a Potential Key for Understanding Prion-Prion Interactions
J. Mol. Biol. 392 (1), 198 - 207