Determination of size of folding nuclei of fibrils formed from recombinant Aβ(1-40) peptide
Determination of size of folding nuclei of fibrils formed from recombinant Aβ(1-40) peptide
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DOI：
10.1134/s0006297916050114
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发表时间：
2016-05-01
影响因子：
2.8
通讯作者：
Galzitskaya, O. V.
中科院分区：
文献类型：
--
作者：
Grigorashvili, E. I.;Selivanova, O. M.;Galzitskaya, O. V.
We have developed a highly efficient method for purification of the recombinant product A beta(1-40) peptide. The concentration dependence of amyloid formation by recombinant A beta(1-40) peptide was studied using fluorescence spectroscopy and electron microscopy. We found that the process of amyloid formation is preceded by lag time, which indicates that the process is nucleation-dependent. Further exponential growth of amyloid fibrils is followed by branching scenarios. Based on the experimental data on the concentration dependence, the sizes of the folding nuclei of fibrils were calculated. It turned out that the size of the primary nucleus is one "monomer" and the size of the secondary nucleus is zero. This means that the nucleus for new aggregates can be a surface of the fibrils themselves. Using electron microscopy, we have demonstrated that fibrils of these peptides are formed by the association of rounded ring structures.
