Peptide Aβ(16-25) Forms Nanofilms in the Process of Its Aggregation

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O. M. Selivanova¹, E. Yu. Gorbunova², L. G. Mustaeva², E. I. Grigorashvili¹, M. Yu. Suvorina¹, A. K. Surin^1,3, and O. V. Galzitskaya^1*

¹Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia; E-mail: ogalzit@vega.protres.ru

²Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia

³State Research Center for Applied Microbiology and Biotechnology, 142279 Obolensk, Moscow Region, Russia

^* To whom correspondence should be addressed.

Received April 4, 2016; Revision received April 8, 2016

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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.

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KEY WORDS: amyloid fibril, protofibril, oligomer, Aβ peptide, Alzheimer’s disease, electron microscopy

DOI: 10.1134/S0006297916070129

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