SMALL ANGLE X-RAY SCATTERING STUDY OF INSULIN FIBRILS

doi:10.26565/2312-4334-2014-4-12

M. V. Romanova Department of Nuclear and Medical Physics, V.N. Karazin Kharkiv National University 4 Svobody Sq., Kharkov, 61022, Ukraine;
I. L. Maliyov Department of Nuclear and Medical Physics, V.N. Karazin Kharkiv National University 4 Svobody Sq., Kharkov, 61022, Ukraine
M. S. Girych Department of Nuclear and Medical Physics, V.N. Karazin Kharkiv National University 4 Svobody Sq., Kharkov, 61022, Ukraine
Kateryna A. Vus Department of Nuclear and Medical Physics, V.N. Karazin Kharkiv National University4 Svobody Sq., Kharkov, 61022, Ukraine; https://orcid.org/0000-0003-4738-4016
Dmitri I. Svergun European Molecular Biology Laboratory (EMBL) Hamburg Outstation, Notkestrasse 85, D22603 Hamburg, Germany. https://orcid.org/0000-0003-0830-5696
Al. Kikhney European Molecular Biology Laboratory (EMBL) Hamburg Outstation, Notkestrasse 85, D22603 Hamburg, Germany. https://orcid.org/0000-0003-1321-3956
C. Jeffries European Molecular Biology Laboratory (EMBL) Hamburg Outstation, Notkestrasse 85, D22603 Hamburg, Germany.

DOI: https://doi.org/10.26565/2312-4334-2014-4-12

Анотація

The small-angle X-ray scattering technique was employed to determine low-resolution 3D structure of insulin amyloid fibrils. This object is of particular interest since amyloid deposits of insulin causes insulin injection amyloidosis. Structural characterization of amyloid fibrils as a particular class of linear highly ordered protein aggregates is of utmost importance for deeper understanding of the molecular etiology of conformational diseases and development of effective therapeutic strategies. The small-angle X-ray scattering pattern analysis showed that the maximum dimension of the insulin fibril cross-section reaches 24±2.4 nm, while gyration radius of the cross-section is about 6 nm.

Завантаження

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Біографія автора

C. Jeffries, European Molecular Biology Laboratory (EMBL) Hamburg Outstation, Notkestrasse 85, D22603 Hamburg, Germany.

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