Determination of regions involved in amyloid fibril formation for Aβ(1-40) peptide
- Авторы: Surin A.1,2, Grigorashvili E.1, Suvorina M.1, Selivanova O.1, Galzitskaya O.1
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Учреждения:
- Institute of Protein Research
- State Research Center for Applied Microbiology and Biotechnology
- Выпуск: Том 81, № 7 (2016)
- Страницы: 762-769
- Раздел: Article
- URL: https://journals.rcsi.science/0006-2979/article/view/150957
- DOI: https://doi.org/10.1134/S0006297916070130
- ID: 150957
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Аннотация
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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Об авторах
A. Surin
Institute of Protein Research; State Research Center for Applied Microbiology and Biotechnology
Email: ogalzit@vega.protres.ru
Россия, Pushchino, Moscow Region, 142290; Obolensk, Moscow Region, 142279
E. Grigorashvili
Institute of Protein Research
Email: ogalzit@vega.protres.ru
Россия, Pushchino, Moscow Region, 142290
M. Suvorina
Institute of Protein Research
Email: ogalzit@vega.protres.ru
Россия, Pushchino, Moscow Region, 142290
O. Selivanova
Institute of Protein Research
Email: ogalzit@vega.protres.ru
Россия, Pushchino, Moscow Region, 142290
O. Galzitskaya
Institute of Protein Research
Автор, ответственный за переписку.
Email: ogalzit@vega.protres.ru
Россия, Pushchino, Moscow Region, 142290
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