Author:
Faridi Nassim,Sanjari-Pour Maryam,Wang Ping,Bathaie S. Zahra
Abstract
AbstractThe 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.
Funder
Tarbiat Modares University
The key projects of international scientific and technological innovation cooperation between governments
Publisher
Springer Science and Business Media LLC
Subject
Organic Chemistry,Biochemistry,Bioengineering,Analytical Chemistry