On the determination of the helical structure parameters of amyloid protofilaments by small-angle neutron scattering and atomic force microscopy

被引：13

作者：

Avdeev, Mikhail V. ^{[1
]}

Aksenov, Victor L. ^{[1
,2
]}

Gazova, Zuzana ^{[3
]}

Almasy, Laszlo ^{[4
]}

Petrenko, Viktor I. ^{[1
,5
]}

Gojzewski, Hubert ^{[6
,7
]}

Feoktystov, Artem V. ^{[8
]}

Siposova, Katarina ^{[3
,9
]}

Antosova, Andrea ^{[3
]}

Timko, Milan ^{[3
]}

Kopcansky, Peter ^{[3
]}

机构：

[1] Joint Inst Nucl Res, Frank Lab Neutron Phys, Dubna 141980, Russia

[2] IV Kurchatov Atom Energy Inst, Natl Res Ctr, Moscow 123182, Russia

[3] Slovak Acad Sci, Inst Expt Phys, Kosice 04001, Slovakia

[4] Inst Solid State Phys & Opt, Wigner RCP, H-1525 Budapest, Hungary

[5] Taras Shevchenko Kyiv Natl Univ, Dept Phys, UA-01601 Kiev, Ukraine

[6] Poznan Univ Tech, Inst Phys, PL-60965 Poznan, Poland

[7] Max Planck Inst Colloids & Interfaces, Dept Interfaces, D-14476 Potsdam, Germany

[8] Forschungszentrum Julich, Julich Ctr Neutron Sci, D-85747 Garching, Germany

[9] Pavol Jozef Safarik Univ, Fac Sci, Dept Biochem, Kosice 04001, Slovakia

来源：

JOURNAL OF APPLIED CRYSTALLOGRAPHY | 2013年 / 46卷

关键词：

X-RAY; FIBRIL FORMATION; LYSOZYME; WATER; BETA(2)-MICROGLOBULIN; FRAGMENT; NUCLEUS; PATHWAY; MODEL; SANS;

D O I：

10.1107/S0021889812050042

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The helical structure of amyloid protofilaments of hen egg white lysozyme was analyzed by small-angle neutron scattering (SANS) and atomic force microscopy (AFM). The structure of these formations in bulk solutions was adequately described by SANS in terms of a simplified model of a helix with spherical structural units. The found main helix parameters (pitch and effective diameter) are consistent with the results of AFM analysis for amyloid fibrils adsorbed on a mica surface. Both methods reveal a strong isotope effect on the structure of amyloid fibrils with respect to the substitution of heavy for light water in the solvent. Specific details responsible for the structural differences when comparing SANS and AFM data are discussed from the viewpoint of methodological aspects, the influence of different (native and adsorbed) amyloid states and sample preparation.

引用

页码：224 / 233

页数：10

共 50 条

[1] Direct Observation of Time-Resolved Polymorphic States in the Self-Assembly of End-Capped Heptapeptides [J].

Adamcik, Jozef ;

Castelletto, Valeria ;

Bolisetty, Sreenath ;

Hamley, Ian W. ;

Mezzenga, Raffaele .

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2011, 50 (24) :5495-5498

[2]

Adamcik J, 2010, NAT NANOTECHNOL, V5, P423, DOI [10.1038/NNANO.2010.59, 10.1038/nnano.2010.59]

[3] Multiple steps during the formation of β-lactoglobulin fibrils [J].

Arnaudov, LN ;

de Vries, R ;

Ippel, H ;

van Mierlo, CPM .

BIOMACROMOLECULES, 2003, 4 (06) :1614-1622

[4] Effect of Fe3O4 magnetic nanoparticles on lysozyme amyloid aggregation [J].

Bellova, Andrea ;

Bystrenova, Eva ;

Koneracka, Martina ;

Kopcansky, Peter ;

Valle, Francesco ;

Tomasovicova, Natalia ;

Timko, Milan ;

Bagelova, Jaroslava ;

Biscarini, Fabio ;

Gazova, Zuzana .

NANOTECHNOLOGY, 2010, 21 (06) :065103

[5] Normal capillary forces [J].

Butt, Hans-Juergen ;

Kappl, Michael .

ADVANCES IN COLLOID AND INTERFACE SCIENCE, 2009, 146 (1-2) :48-60

[6] Ultrastructural organization of amyloid fibrils by atomic force microscopy [J].

Chamberlain, AK ;

MacPhee, CE ;

Zurdo, J ;

Morozova-Roche, LA ;

Hill, HAO ;

Dobson, CM ;

Davis, JJ .

BIOPHYSICAL JOURNAL, 2000, 79 (06) :3282-3293

[7] THE LEADING ASYMPTOTIC TERM OF THE SMALL-ANGLE INTENSITIES SCATTERED BY SOME IDEALIZED SYSTEMS [J].

CICCARIELLO, S .

JOURNAL OF APPLIED CRYSTALLOGRAPHY, 1991, 24 :509-515

[8] Amyloid fibrils of glucagon characterized by high-resolution atomic force microscopy [J].

De Jong, Kathy L. ;

Incledon, Bev ;

Yip, Christopher M. ;

DeFelippis, Michael R. .

BIOPHYSICAL JOURNAL, 2006, 91 (05) :1905-1914

[9] AFM study of glucagon fibrillation via oligomeric structures resulting in interwoven fibrils [J].

Dong, Mingdong ;

Hovgaard, Mads Bruun ;

Xu, Sailong ;

Otzen, Daniel Erik ;

Besenbacher, Flemming .

NANOTECHNOLOGY, 2006, 17 (16) :4003-4009

[10] A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme [J].

Dumoulin, M ;

Last, AM ;

Desmyter, A ;

Decanniere, K ;

Canet, D ;

Larsson, G ;

Spencer, A ;

Archer, DB ;

Sasse, J ;

Muyldermans, S ;

Wyns, L ;

Redfield, C ;

Matagne, A ;

Robinson, CV ;

Dobson, CM .

NATURE, 2003, 424 (6950) :783-788

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