On the structural definition of amyloid fibrils and other polypeptide aggregates

被引:201
作者
Faendrich, M. [1 ]
机构
[1] Leibniz Inst Altersforsch, D-07745 Jena, Germany
关键词
amyloid; conformational disease; misfolding; prion; protein folding;
D O I
10.1007/s00018-007-7110-2
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
Amyloid fibrils occur inside the human body, associated with ageing or a group of diseases that includes, amongst others, Alzheimer's disease, atherosclerosis and type II diabetes. Many natural polypeptide chains are able to form amyloid fibrils in vivo or in vitro, and this ability has been suggested to represent an inherent consequence of the chemical structure of the polypeptide chain. Recent literature has provided a wealth of information about the structure of aggregates, precipitates, amyloid fibrils and other types of fibrillar polypeptide assemblies. However, the biophysical meaning associated with these terms can differ considerably depending on the context of their usage. This overview presents a structural comparison of amyloid fibrils and other types of polypeptide assemblies and defines amyloid fibrils, based on structural considerations, as fibrillar polypeptide aggregates with a cross-beta conformation.
引用
收藏
页码:2066 / 2078
页数:13
相关论文
共 106 条
[11]  
Cantor EJ, 1997, J BIOCHEM, V122, P217
[12]   Cell toxicity and conformational disease [J].
Carrell, RW .
TRENDS IN CELL BIOLOGY, 2005, 15 (11) :574-580
[13]   Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders [J].
Caughey, B ;
Lansbury, PT .
ANNUAL REVIEW OF NEUROSCIENCE, 2003, 26 :267-298
[14]   Structural stability of amyloid fibrils of β2-microglobulin in comparison with its native fold [J].
Chatani, E ;
Goto, Y .
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 2005, 1753 (01) :64-75
[15]   Protein misfolding, functional amyloid, and human disease [J].
Chiti, Fabrizio ;
Dobson, Christopher M. .
ANNUAL REVIEW OF BIOCHEMISTRY, 2006, 75 :333-366
[16]   In situ characterization of beta-amyloid in Alzheimer's diseased tissue by synchrotron Fourier transform infrared Microspectroscopy [J].
Choo, LP ;
Wetzel, DL ;
Halliday, WC ;
Jackson, M ;
LeVine, SM ;
Mantsch, HH .
BIOPHYSICAL JOURNAL, 1996, 71 (04) :1672-1679
[17]   CONFORMATION OF TWISTED BETA-PLEATED SHEETS IN PROTEINS [J].
CHOTHIA, C .
JOURNAL OF MOLECULAR BIOLOGY, 1973, 75 (02) :295-302
[18]   Mutagenic analysis of the nucleation propensity of oxidized Alzheimer's β-amyloid peptide [J].
Christopeit, T ;
Hortschansky, P ;
Schroeckh, V ;
Gührs, K ;
Zandomeneghi, G ;
Fändrich, M .
PROTEIN SCIENCE, 2005, 14 (08) :2125-2131
[19]   ELECTRON MICROSCOPIC OBSERVATIONS ON A FIBROUS COMPONENT IN AMYLOID OF DIVERSE ORIGINS [J].
COHEN, AS ;
CALKINS, E .
NATURE, 1959, 183 (4669) :1202-1203
[20]  
COHEN AS, 1969, P S AMYLOISDOSIS, P149