The Effect of Ultrasonication on the Fibrillar/ Oligomeric Structures of Aβ at Different Concentrations

Overview

Journal Protein J

Publisher Springer

Specialty Biochemistry

Date 2023 Aug 27

PMID 37634212

Authors

Nassim Faridi

Maryam Sanjari-Pour

Ping Wang

S Zahra Bathaie

Affiliations

Soon will be listed here.

Abstract

The number of disease states linked the aberrant regular protein conformations to oligomers and amyloid fibrils. Amyloid beta 1-42 (Aβ) 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 Aβ peptides of different sizes and oligomers. Herein, we investigated the effects of buffer and ultrasonication on Aβ structure at low and high concentrations. After ultrasonication, the Western blot results showed that Aβ fibrils were disaggregated into different sizes. The transmission electron microscopy results indicated Aβ at low concentration (25 µM) in Ham's/F12 phenol red-free culture medium formed short-size fragments and oligomers. In comparison, Aβ 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 Aβ 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 Aβ aggregates with a particular size and molecular structure.

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