Examining the structure of the mature amyloid fibril

被引:56
作者
Makin, OS [1 ]
Serpell, LC [1 ]
机构
[1] Cambridge Inst Med Res, Struct Med Unit, Cambridge CB2 2XY, England
关键词
diffraction; electron microscopy; NMR;
D O I
10.1042/bst0300521
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
The pathogenesis of the group of diseases known collectively as the amyloidoses is characterized by the deposition of insoluble amyloid fibrils. These are straight, unbranching structures about 120 Angstrom (1 Angstrom = 0.1 nm) in diameter and of indeterminate length formed by the self-assembly of a diverse group of normally soluble proteins. Knowledge of the structure of these fibrils is necessary for the understanding of their abnormal assembly and deposition, possibly leading to the rational design of therapeutic agents for their prevention or disaggregation. Structural elucidation is impeded by fibril insolubility and inability to crystallize, thus preventing the use of X-ray crystallography and solution NMR. CD, Fourier-transform infrared spectroscopy and light scattering have been used in the study of the mechanism of fibril formation. This review concentrates on the structural information about the final, mature fibril and in particular the complementary techniques of cryo-electron microscopy, solid-state NMR and X-ray fibre diffraction.
引用
收藏
页码:521 / 525
页数:5
相关论文
共 33 条
[21]   X-RAY-DIFFRACTION FROM INTRANEURONAL PAIRED HELICAL FILAMENTS AND EXTRANEURONAL AMYLOID FIBERS IN ALZHEIMER-DISEASE INDICATES CROSS-BETA CONFORMATION [J].
KIRSCHNER, DA ;
ABRAHAM, C ;
SELKOE, DJ .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1986, 83 (02) :503-507
[22]   STRUCTURAL MODEL FOR THE BETA-AMYLOID FIBRIL BASED ON INTERSTRAND ALIGNMENT OF AN ANTIPARALLEL-SHEET COMPRISING A C-TERMINAL PEPTIDE [J].
LANSBURY, PT ;
COSTA, PR ;
GRIFFITHS, JM ;
SIMON, EJ ;
AUGER, M ;
HALVERSON, KJ ;
KOCISKO, DA ;
HENDSCH, ZS ;
ASHBURN, TT ;
SPENCER, RGS ;
TIDOR, B ;
GRIFFIN, RG .
NATURE STRUCTURAL BIOLOGY, 1995, 2 (11) :990-998
[23]   Structural analysis of Alzheimer's β(1-40) amyloid:: Protofilament assembly of tubular fibrils [J].
Malinchik, SB ;
Inouye, H ;
Szumowski, KE ;
Kirschner, DA .
BIOPHYSICAL JOURNAL, 1998, 74 (01) :537-545
[24]   X-RAY-DIFFRACTION OF SCRAPIE PRION RODS AND PRP PEPTIDES [J].
NGUYEN, JT ;
INOUYE, H ;
BALDWIN, MA ;
FLETTERICK, RJ ;
COHEN, FE ;
PRUSINER, SB ;
KIRSCHNER, DA .
JOURNAL OF MOLECULAR BIOLOGY, 1995, 252 (04) :412-422
[25]   CONFIGURATIONS OF POLYPEPTIDE CHAINS WITH FAVORED ORIENTATIONS AROUND SINGLE BONDS - 2 NEW PLEATED SHEETS [J].
PAULING, L ;
COREY, RB .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1951, 37 (11) :729-740
[26]   ON BINDING OF CONGO RED BY AMYLOID [J].
PUCHTLER, H ;
SWEAT, F ;
LEVINE, M .
JOURNAL OF HISTOCHEMISTRY & CYTOCHEMISTRY, 1962, 10 (03) :355-&
[27]   Molecular structure of a fibrillar Alzheimer's Aβ fragment [J].
Serpell, LC ;
Blake, CCF ;
Fraser, PE .
BIOCHEMISTRY, 2000, 39 (43) :13269-13275
[28]   Direct visualisation of the β-sheet structure of synthetic Alzheimer's amyloid [J].
Serpell, LC ;
Smith, JM .
JOURNAL OF MOLECULAR BIOLOGY, 2000, 299 (01) :225-231
[29]   Alzheimer's amyloid fibrils: structure and assembly [J].
Serpell, LC .
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE, 2000, 1502 (01) :16-30
[30]   HIGH-RESOLUTION ELECTRON MICROSCOPIC ANALYSIS OF AMYLOID FIBRIL [J].
SHIRAHAMA, T ;
COHEN, AS .
JOURNAL OF CELL BIOLOGY, 1967, 33 (03) :679-+