Peptide Aβ(16-25) forms nanofilms in the process of its aggregation


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Resumo

A method for the synthesis and high purification of fragments of Aβ(1-42) peptide has been elaborated. We have synthesized the amyloidogenic fragment Aβ(16-25) predicted by us and studied the process of its aggregation by electron microscopy and X-ray analysis. Electron microscopy images show that the peptide forms a film, which is not characteristic of amyloid fibrils. At the same time, according to the X-ray diffraction data, its preparations display the presence of two main reflections (4.6-4.8 and 8-12 Å) characteristic of cross-β structure of amyloid fibrils. Thus, the fragment Aβ(16-25) that we predicted is a promising object not only for studying the process of polymerization of the peptides/proteins, but also for using it as a nanomaterial to study a number of biological processes.

Sobre autores

O. Selivanova

Institute of Protein Research

Email: ogalzit@vega.protres.ru
Rússia, Pushchino, Moscow Region, 142290

E. Gorbunova

Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry

Email: ogalzit@vega.protres.ru
Rússia, Pushchino, Moscow Region, 142290

L. Mustaeva

Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry

Email: ogalzit@vega.protres.ru
Rússia, Pushchino, Moscow Region, 142290

E. Grigorashvili

Institute of Protein Research

Email: ogalzit@vega.protres.ru
Rússia, Pushchino, Moscow Region, 142290

M. Suvorina

Institute of Protein Research

Email: ogalzit@vega.protres.ru
Rússia, Pushchino, Moscow Region, 142290

A. Surin

Institute of Protein Research; State Research Center for Applied Microbiology and Biotechnology

Email: ogalzit@vega.protres.ru
Rússia, Pushchino, Moscow Region, 142290; Obolensk, Moscow Region, 142279

O. Galzitskaya

Institute of Protein Research

Autor responsável pela correspondência
Email: ogalzit@vega.protres.ru
Rússia, Pushchino, Moscow Region, 142290


Declaração de direitos autorais © Pleiades Publishing, Ltd., 2016

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