Ultrastructural organization of amyloid fibrils by atomic force microscopy

被引:164
|
作者
Chamberlain, AK
MacPhee, CE
Zurdo, J
Morozova-Roche, LA
Hill, HAO
Dobson, CM
Davis, JJ
机构
[1] Univ Oxford, Oxford Ctr Mol Sci, New Chem Lab, Oxford OX1 3QT, England
[2] Univ Oxford, Inorgan Chem Lab, Oxford OX1 3QT, England
基金
英国生物技术与生命科学研究理事会; 英国医学研究理事会; 英国惠康基金; 英国工程与自然科学研究理事会;
关键词
D O I
10.1016/S0006-3495(00)76560-X
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
Atomic force microscopy has been employed to investigate the structural organization of amyloid fibrils produced in vitro from three very different polypeptide sequences. The systems investigated are a 10-residue peptide derived from the sequence of transthyretin, the 90-residue SH3 domain of bovine phosphatidylinositol-3'-kinase, and human wild-type lysozyme, a 130-residue protein containing four disulfide bridges. The results demonstrate distinct similarities between the structures formed by the different classes of fibrils despite the contrasting nature of the polypeptide species involved. SH3 and lysozyme fibrils consist typically of four protofilaments, exhibiting a left-handed twist along the fibril axis. The substructure of TTR10-19 fibrils is not resolved by atomic force microscopy and their uniform appearance is suggestive of a regular self-association of very thin filaments. We propose that the exact number and orientation of protofilaments within amyloid fibrils is dictated by packing of the regions of the polypeptide chains that are not directly involved in formation of the cross-beta core of the fibrils. The results obtained for these proteins, none of which is directly associated with any human disease, are closely similar to those of disease-related amyloid fibrils, supporting the concept that amyloid is a generic structure of polypeptide chains. The detailed architecture of an individual fibril, however, depends on the manner in which the protofilaments assemble into the fibrillar structure, which in turn is dependent on the sequence of the polypeptide and the conditions under which the fibril is formed.
引用
收藏
页码:3282 / 3293
页数:12
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