超声对不同浓度Aβ1−42纤维/寡聚体结构的影响

IF 1.9 4区 生物学 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY The Protein Journal Pub Date : 2023-08-27 DOI:10.1007/s10930-023-10138-0
Nassim Faridi, Maryam Sanjari-Pour, Ping Wang, S. Zahra Bathaie
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引用次数: 0

摘要

疾病状态的数量将异常的规则蛋白质构象与低聚物和淀粉样原纤维联系起来。淀粉样蛋白β 1-42 (a - β1−42)肽具有很强的疏水性,在某些溶液和缓冲条件下迅速形成富β结构和纤维蛋白聚集体。超声脉冲可以将淀粉样蛋白原纤维破坏成更小的片段,并产生不同大小的a - β1 - 42肽和低聚物。在此,我们研究了缓冲液和超声波对低浓度和高浓度Aβ1−42结构的影响。超声处理后,Western blot结果显示a - β1−42原纤维被分解成不同大小。透射电镜结果显示,低浓度(25µM)的Aβ1−42在Ham’s/F12无酚红培养基中形成短片段和低聚物。相比之下,a - β1−42在较高浓度(100µM)下形成原纤维,超声作用后成更小的碎片。然而,再生后,它又形成了成熟的原纤维。细胞活力测定表明,低浓度(25µM)形成的a - β1−42寡聚物对PC12细胞的毒性大于其他形式。综上所述,通过施加超声脉冲,控制肽浓度和缓冲条件,可以丰富具有特定大小和分子结构的a β1−42聚集体。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

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The Effect of Ultrasonication on the Fibrillar/ Oligomeric Structures of Aβ1−42 at Different Concentrations

The number of disease states linked the aberrant regular protein conformations to oligomers and amyloid fibrils. Amyloid beta 1–42 (Aβ1−42) peptide is very hydrophobic and quickly forms the β-rich structure and fibrillar protein aggregates in some solutions and buffer conditions. Ultrasonication pulses can disrupt amyloid fibrils to smaller fragments and produce Aβ1−42 peptides of different sizes and oligomers. Herein, we investigated the effects of buffer and ultrasonication on Aβ1−42 structure at low and high concentrations. After ultrasonication, the Western blot results showed that Aβ1−42 fibrils were disaggregated into different sizes. The transmission electron microscopy results indicated Aβ1−42 at low concentration (25 µM) in Ham’s/F12 phenol red-free culture medium formed short-size fragments and oligomers. In comparison, Aβ1−42 at higher concentration (100 µM) formed fibrils that break down into smaller fragments after ultrasonication. However, after regrowth, it formed mature fibrils again. Cell viability assay indicated that Aβ1−42 oligomers formed at a low concentration (25 µM) were more toxic to PC12 cells than other forms. In conclusion, by applying ultrasonication pulses and controlling peptide concentration and buffer condition, we can rich Aβ1−42 aggregates with a particular size and molecular structure.

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来源期刊
The Protein Journal
The Protein Journal 生物-生化与分子生物学
CiteScore
5.20
自引率
0.00%
发文量
57
审稿时长
12 months
期刊介绍: The Protein Journal (formerly the Journal of Protein Chemistry) publishes original research work on all aspects of proteins and peptides. These include studies concerned with covalent or three-dimensional structure determination (X-ray, NMR, cryoEM, EPR/ESR, optical methods, etc.), computational aspects of protein structure and function, protein folding and misfolding, assembly, genetics, evolution, proteomics, molecular biology, protein engineering, protein nanotechnology, protein purification and analysis and peptide synthesis, as well as the elucidation and interpretation of the molecular bases of biological activities of proteins and peptides. We accept original research papers, reviews, mini-reviews, hypotheses, opinion papers, and letters to the editor.
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