Atomic structure and hierarchical assembly of a cross-β amyloid fibril

被引：450

作者：

Fitzpatrick, Anthony W. P. ^{[1
,2
]}

Debelouchina, Galia T. ^{[3
,4
]}

Bayro, Marvin J. ^{[3
,4
]}

Clare, Daniel K. ^{[5
]}

Caporini, Marc A. ^{[3
,4
]}

Bajaj, Vikram S. ^{[3
,4
]}

Jaroniec, Christopher P. ^{[3
,4
]}

Wang, Luchun ^{[5
]}

Ladizhansky, Vladimir ^{[3
,4
]}

Mueller, Shirley A. ^{[6
]}

MacPhee, Cait E. ^{[7
]}

Waudby, Christopher A. ^{[1
,5
]}

Mott, Helen R. ^{[8
]}

De Simone, Alfonso ^{[1
,9
]}

Knowles, Tuomas P. J. ^{[1
]}

Saibil, Helen R. ^{[5
]}

Vendruscolo, Michele ^{[1
]}

Orlova, Elena V. ^{[5
]}

Griffin, Robert G. ^{[3
,4
]}

Dobson, Christopher M. ^{[1
]}

机构：

[1] Univ Cambridge, Dept Chem, Cambridge CB2 1EW, England

[2] Univ Cambridge, Cavendish Lab, Cambridge CB3 0HE, England

[3] MIT, Francis Bitter Magnet Lab, Cambridge, MA 02139 USA

[4] MIT, Dept Chem, Cambridge, MA 02139 USA

[5] Univ London Birkbeck Coll, Inst Struct & Mol Biol, London WC1E 7HX, England

[6] Biozentrum, Maurice E Muller Inst, CH-4056 Basel, Switzerland

[7] Univ Edinburgh, Sch Phys, Edinburgh EH9 3JZ, Midlothian, Scotland

[8] Univ Cambridge, Dept Biochem, Cambridge CB2 1GA, England

[9] Univ London Imperial Coll Sci Technol & Med, Div Mol Biosci, London SW7 2AZ, England

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2013年 / 110卷 / 14期

基金：

英国工程与自然科学研究理事会; 美国国家卫生研究院; 英国生物技术与生命科学研究理事会; 瑞士国家科学基金会; 英国惠康基金;

关键词：

MODEL; STATE; A-BETA(1-40); DISTANCES; PEPTIDES; PROTEINS; REVEALS; C-13;

D O I：

10.1073/pnas.1219476110

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The cross-beta amyloid form of peptides and proteins represents an archetypal and widely accessible structure consisting of ordered arrays of beta-sheet filaments. These complex aggregates have remarkable chemical and physical properties, and the conversion of normally soluble functional forms of proteins into amyloid structures is linked to many debilitating human diseases, including several common forms of age-related dementia. Despite their importance, however, cross-beta amyloid fibrils have proved to be recalcitrant to detailed structural analysis. By combining structural constraints from a series of experimental techniques spanning five orders of magnitude in length scale-including magic angle spinning nuclear magnetic resonance spectroscopy, X-ray fiber diffraction, cryoelectron microscopy, scanning transmission electron microscopy, and atomic force microscopy-we report the atomic-resolution (0.5 angstrom) structures of three amyloid polymorphs formed by an 11-residue peptide. These structures reveal the details of the packing interactions by which the constituent beta-strands are assembled hierarchically into protofilaments, filaments, and mature fibrils.

引用

页码：5468 / 5473

页数：6

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