NR ACKI
AU Caughey,B.W.; Dong,A.; Bhat,K.S.; Ernst,D.; Hayes,S.F.; Caughey,W.S.
TI Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy
QU Biochemistry 1991 Aug 6; 30(31): 7672-80
ER Biochemistry 1991 Oct 29;30(43):10600
PT journal article
AB A protease-resistant form of the protein PrP (PrPres) accumulates in tissues of mammals infected with scrapie, Creutzfeldt-Jakob disease, and related transmissible neurodegenerative diseases. This abnormal form of PrP can aggregate into insoluble amyloid-like fibrils and plaques and has been identified as the major component of brain fractions enriched for scrapie infectivity. Using a recently developed technique in Fourier transform infrared spectroscopy which allows protein conformational analysis in aqueous media, we have studied the secondary structure of the proteinase K resistant core of PrPres (PrPres 27-30) as it exists in highly infectious fibril preparations. Second-derivative analysis of the infrared spectra has enabled us to quantitate the relative amounts of different secondary structures in the PrPres aggregates. The analysis indicated that PrPres 27-30 is predominantly composed of beta-sheet (47%), which is consistent with its amyloid-like properties. In addition, significant amounts of turn (31%) and alpha-helix (17%) were identified, indicating that amyloid-like fibrils need not be exclusively beta-sheet. The infrared-based secondary structure compositions were then used as constraints to improve the theoretical localization of the secondary structures within PrPres 27-30.
IN Eine proteaseresistante Form des Proteins PrP (PrPres) akkumuliert in mit Scrapie-, Creutzfeldt-Jakob- oder verwandten Erregern infizierten Geweben und aggregiert zu unlöslichen amyloidähnlichen Fibrillen. Dieses modifizierte Protein ist die Hauptkomponente für den Scrapieerreger angereicherter Fraktionen. Durch Fouriertransformation ausgewertete Infrarotspektroskopie in wässrigem Medium deutet darauf hin, dass PrPres 27-30 zu 47% aus Betafaltblättern, zu 31% aus Turns und zu 17% aus Alphahelices besteht.
MH Acetylglucosamine/chemistry; Animal; Brain/microbiology; Electrophoresis, Polyacrylamide Gel; Hamsters; Mesocricetus; Microscopy, Electron; Molecular Weight; PrP 27-30 Protein; Prions/*metabolism; Protein Conformation; Scrapie/microbiology; Spectrophotometry, Infrared; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Viral Proteins/biosynthesis/*chemistry/isolation &; purification/ultrastructure; Water
AD Byron W. Caughey, Kolari S. Bhat, Darwin Ernst, Stanley F. Hayes, NIAID, National Institutes of Health, Rocky Mountain Laboratories, Hamilton, Montana 59840; Aichun Dong, Winslow S. Caughey, Department of Biochemistry, Colorado State University, Ft. Collins, Colorado 80523
SP englisch
PO USA