SMALL ANGLE X-RAY SCATTERING STUDY OF INSULIN FIBRILS

Autor: M. V. Romanova, I. L. Maliyov, M. S. Girych, E. A. Vus, D. I. Svergun, Al. Kikhney, C. Jeffries
Jazyk: English<br />Russian<br />Ukrainian
Rok vydání: 2015
Předmět:
Zdroj: East European Journal of Physics, Vol 1, Iss 4, Pp 96-99 (2015)
Druh dokumentu: article
ISSN: 2312-4334
2312-4539
Popis: 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.
Databáze: Directory of Open Access Journals