STRUCTURAL STUDIES OF TAU-PROTEIN AND ALZHEIMER PAIRED HELICAL FILAMENTS SHOW NO EVIDENCE FOR BETA-STRUCTURE

被引：0

作者：

SCHWEERS, O ^{[1
]}

SCHONBRUNNHANEBECK, E ^{[1
]}

MARX, A ^{[1
]}

MANDELKOW, E ^{[1
]}

机构：

[1] DESY, MAX PLANCK UNIT STRUCT MOLEC BIOL, D-22603 HAMBURG, GERMANY

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 1994年 / 269卷 / 39期

关键词：

D O I：

暂无

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：

We have studied the conformation of tau protein and Alzheimer paired helical filaments (PHF) by several spectroscopic, scattering, and imaging methods revealing the overall shape and the conformation of the polypeptide backbone. Tau protein behaves in solution as if it were denatured; no evidence for compact folding was detected. The protein is highly extended, there is no defined radius of gyration, and the scattering is best described by that of a random (''Gaussian'') polymer. CD and Fourier transform infrared spectroscopy show only a minimal content of ordered secondary structure (alpha-helix or beta-sheet). Similarly, PHFs from Alzheimer brain tissue show no detectable secondary structure by x-ray diffraction or spectroscopy. It is thus unlikely that the aggregation of tau into Alzheimer PHFs is based on interactions between strands of beta-sheets (a model currently favored for other disease-related polymers such as beta-amyloid fibers of Alzheimer's disease).

引用

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页码：24290 / 24297

页数：8

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