SECONDARY STRUCTURE-ANALYSIS OF THE SCRAPIE-ASSOCIATED PROTEIN PRP 27-30 IN WATER BY INFRARED-SPECTROSCOPY

被引：737

作者：

CAUGHEY, BW ^{[1
]}

DONG, A ^{[1
]}

BHAT, KS ^{[1
]}

ERNST, D ^{[1
]}

HAYES, SF ^{[1
]}

CAUGHEY, WS ^{[1
]}

机构：

[1] COLORADO STATE UNIV,DEPT BIOCHEM,FT COLLINS,CO 80523

来源：

BIOCHEMISTRY | 1991年 / 30卷 / 31期

关键词：

D O I：

10.1021/bi00245a003

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A protease-resistant form of the protein PrP (PrP-res) 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 PrP-res (PrP-res 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 PrP-res aggregates. The analysis indicated that PrP-res 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 PrP-res 27-30.

引用

页码：7672 / 7680

页数：9

共 70 条

[1] DOES AGENT OF SCRAPIE REPLICATE WITHOUT NUCLEIC ACID [J].