Sequence and structural determinants of amyloid fibril formation

被引：89

作者：

Bemporad, Francesco ^{[1
]}

Calloni, Giulia ^{[1
]}

Campioni, Silvia ^{[1
]}

Plakoutsi, Georgia ^{[1
]}

Taddei, Niccolo ^{[1
]}

Chiti, Fabrizio ^{[1
]}

机构：

[1] Univ Florence, Dipartimento Sci Biochim, I-50134 Florence, Italy

来源：

ACCOUNTS OF CHEMICAL RESEARCH | 2006年 / 39卷 / 09期

关键词：

D O I：

10.1021/ar050067x

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Amyloid fibril formation is a process that represents an essential feature of the chemistry of proteins and plays a central role in human pathology and the biology of living organisms. In this Account, we shall describe some of the recent results on the sequence and structural determinants of protein aggregation. We shall describe the factors that govern aggregation of unfolded peptides and proteins. We shall then try to summarize the factors that pertain to the aggregation of partially structured states and will show that even fully folded states of proteins have an ability to aggregate into at least early oligomers with no need to undergo substantial conformational changes.

引用

页码：620 / 627

页数：8

共 42 条

[11] Mutagenesis of the central hydrophobic cluster in Aβ42 Alzheimer's pepticle -: Side-chain properties correlate with aggregation propensities
de Groot, NS
Aviles, FX
Vendrell, J
Ventura, S
[J]. FEBS JOURNAL, 2006, 273 (03) : 658 - 668
[12] Structure and properties of α-synuclein and other amyloids determined at the amino acid level
Del Mar, C
Greenbaum, EA
Mayne, L
Englander, SW
Woods, VL
[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2005, 102 (43) : 15477 - 15482
[13] Structural organization of α-synuclein fibrils studied by site-directed spin labeling
Der-Sarkissian, A
Jao, CC
Chen, J
Langen, R
[J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (39) : 37530 - 37535
[14] Protein folding and misfolding
Dobson, CM
[J]. NATURE, 2003, 426 (6968) : 884 - 890
[15] Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains
Dubay, KF
Pawar, AP
Chiti, F
Zurdo, J
Dobson, CM
Vendruscolo, M
[J]. JOURNAL OF MOLECULAR BIOLOGY, 2004, 341 (05) : 1317 - 1326
[16] Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments
Fändrich, M
Forge, V
Buder, K
Kittler, M
Dobson, CM
Diekmann, S
[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2003, 100 (26) : 15463 - 15468
[17] Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
Fernandez-Escamilla, AM
Rousseau, F
Schymkowitz, J
Serrano, L
[J]. NATURE BIOTECHNOLOGY, 2004, 22 (10) : 1302 - 1306
[18] A toy model for predicting the rate of amyloid formation from unfolded protein
Hall, D
Hirota, N
Dobson, CM
[J]. JOURNAL OF MOLECULAR BIOLOGY, 2005, 351 (01) : 195 - 205
[19] Molecular-level secondary structure, polymorphism, and dynamics of full-length α-synuclein fibrils studied by solid-state NMR
Heise, H
Hoyer, W
Becker, S
Andronesi, OC
Riedel, D
Baldus, M
[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2005, 102 (44) : 15871 - 15876
[20] Hölscher C, 1998, J VIROL, V72, P1153

← 1 2 3 4 5 →