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


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Abstract

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.

About the authors

O. M. Selivanova

Institute of Protein Research

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

E. Yu. Gorbunova

Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry

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

L. G. Mustaeva

Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry

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

E. I. Grigorashvili

Institute of Protein Research

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

M. Yu. Suvorina

Institute of Protein Research

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

A. K. Surin

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

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

O. V. Galzitskaya

Institute of Protein Research

Author for correspondence.
Email: ogalzit@vega.protres.ru
Russian Federation, Pushchino, Moscow Region, 142290


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