TY  - JOUR
AU  - Rehders, D.
AU  - Claasen, B.
AU  - Redecke, L.
AU  - Buschke, A.
AU  - Reibe, C.
AU  - Jehmlich, N.
AU  - von Bergen, M.
AU  - Betzel, C.
AU  - Meyer, B.
AU  - DESY
TI  - Peptide NMHRYPNQ of the cellular prion protein (PrP(C)) inhibits aggregation and is a potential key for understanding prion-prion interactions.
JO  - Journal of molecular biology
VL  - 392
SN  - 0022-2836
CY  - Amsterdam [u.a.]
PB  - Elsevier
M1  - PHPPUBDB-19404
SP  - 198-207
PY  - 2009
N1  - © Elsevier Ltd.; Post referee fulltext in progress 2; Embargo 12 months from publication
AB  - Pathogenesis of transmissible spongiform encephalopathies is correlated with a conversion of the normal cellular form of the prion protein (PrP(C)) 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 PrP(C) for binding affinity to PrP(C). Two fragments with binding affinity, 149YYRENMHR156 and 153NMHRYPNQ160, were identified with K(d) values of 21 and 25 microM, respectively. A 10-fold excess of peptide 153NMHRYPNQ160 inhibits aggregation of the PrP by 99
KW  - Drug Evaluation, Preclinical
KW  - Humans
KW  - Kinetics
KW  - Magnetic Resonance Spectroscopy
KW  - Mass Spectrometry
KW  - Models, Molecular
KW  - Peptide Library
KW  - Peptides: pharmacology
KW  - Prions: antagonists & inhibitors
KW  - Prions: metabolism
KW  - Protein Binding
KW  - Protein Structure, Tertiary
KW  - Peptide Library (NLM Chemicals)
KW  - Peptides (NLM Chemicals)
KW  - Prions (NLM Chemicals)
LB  - PUB:(DE-HGF)16
C6  - pmid:19607841
UR  - <Go to ISI:>//WOS:000270123600016
DO  - DOI:10.1016/j.jmb.2009.07.014
UR  - https://bib-pubdb1.desy.de/record/94432
ER  -