NDLI: Characterization of prion protein (PrP)-derived peptides that discriminate full-length PrPSc from PrPC

Content Provider	PubMed Central
Author	Lau, Anthony L. Yam, Alice Y. Michelitsch, Melissa M. D. Wang, Xuemei Gao, Carol Goodson, Robert J. Shimizu, Robert Timoteo, Gulliver Hall, John Angelica, Medina-selby Coit, Doris Mccoin, Colin Phelps, Bruce Wu, Ping Hu, Celine Chien, David Peretz, David
Copyright Year	2007
Abstract	On our initial discovery that prion protein (PrP)-derived peptides were capable of capturing the pathogenic prion protein (PrPSc), we have been interested in how these peptides interact with PrPSc. After screening peptides from the entire human PrP sequence, we found two peptides (PrP19–30 and PrP100–111) capable of binding full-length PrPSc in plasma, a medium containing a complex mixture of other proteins including a vast excess of the normal prion protein (PrPC). The limit of detection for captured PrPSc was calculated to be 8 amol from a ≈105-fold dilution of 10% (wt/vol) human variant Creutzfeldt–Jakob disease brain homogenate, with >3,800-fold binding specificity to PrPSc over PrPC. Through extensive analyses, we show that positively charged amino acids play an important, but not exclusive, role in the interaction between the peptides and PrPSc. Neither hydrophobic nor polar interactions appear to correlate with binding activity. The peptide–PrPSc interaction was not sequence-specific, but amino acid composition affected binding. Binding occurs through a conformational domain that is only present in PrPSc, is species-independent, and is not affected by proteinase K digestion. These and other findings suggest a mechanism by which cationic domains of PrPC may play a role in the recruitment of PrPC to PrPSc.
Related Links	http://dx.doi.org/10.1073/pnas.0704260104
Ending Page	11556
Page Count	6
Starting Page	11551
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	28
Volume Number	104
Language	English
Publisher	National Academy of Sciences
Publisher Date	2007-07-10
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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