Determination of Regions Involved in Amyloid Fibril Formation for Aβ(1-40) Peptide

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A. K. Surin^1,2, E. I. Grigorashvili¹, M. Yu. Suvorina¹, O. M. Selivanova¹, and O. V. Galzitskaya^1*

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

²State Research Center for Applied Microbiology and Biotechnology, 142279 Obolensk, Moscow Region, Russia; E-mail: alan@vega.protres.ru

^* To whom correspondence should be addressed.

Received April 7, 2016; Revision received April 18, 2016

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The studies of amyloid structures and the process of their formation are important problems of biophysics. One of the aspects of such studies is to determine the amyloidogenic regions of a protein chain that form the core of an amyloid fibril. We have theoretically predicted the amyloidogenic regions of the Aβ(1-40) peptide capable of forming an amyloid structure. These regions are from 16 to 21 and from 32 to 36 amino acid residues. In this work, we have attempted to identify these sites experimentally by the method of tandem mass spectrometry. As a result, we show that regions of the Aβ(1-40) peptide from 16 to 22 and from 28 to 40 amino acid residues are resistant to proteases, i.e. they are included in the core of amyloid fibrils. Our results correlate with the results of the theoretical prediction.

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KEY WORDS: Aβ peptide, amyloid fibril, amyloidogenic regions, mass spectrometry, Alzheimer’s disease

DOI: 10.1134/S0006297916070130

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