Details zur Publikation
Kategorie Textpublikation
Referenztyp Zeitschriften
DOI 10.1016/j.jmb.2009.07.014
Titel (primär) Peptide NMHRYPNQ of the Cellular Prion Protein (PrPC) Inhibits Aggregation and Is a Potential Key for Understanding Prion-Prion Interactions
Autor Rehders, D.; Classen, B.; Redecke, L.; Buschke, A.; Reibe, C.; Jehmlich, N. ORCID logo ; von Bergen, M.; Betzel, A.; Meyer, B.
Quelle Journal of Molecular Biology
Erscheinungsjahr 2009
Department METABOX; PROTEOM
Band/Volume 392
Heft 1
Seite von 198
Seite bis 207
Sprache 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.
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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 10.1016/j.jmb.2009.07.014