Low frequency vortex magnetic field reduces amyloid β aggregation, increase cell viability and protect from amyloid β toxicity

Electromagn Biol Med. 2021 Jan 2;40(1):191-200. doi: 10.1080/15368378.2020.1830288. Epub 2020 Oct 12.

Abstract

Plaques formed by abnormal accumulation of amyloid β-peptide (Aβ) lead to onset of Alzheimer's disease (AD). Pharmacological treatments do not reduce Aβ aggregation neither restore learning and memory. Noninvasive techniques have emerged as an alternative to treat AD, such as stimulation with electromagnetic fields (EMF) that decrease Aβ deposition and reverses cognitive impairment in AD mice, even though some studies showed side effects on parallel magnetic fields stimulation. As a new approach of magnetic field (MF) stimulation, vortex magnetic fields (VMF) have been tested inducing a random movement of charged biomolecules in cells, promoting cell viability and apparently safer than parallel magnetic fields. In this study we demonstrate the effect of VMF on Aβ aggregation. The experimental strategy includes, i) design and construction of a coil capable to induce VMF, ii) evaluation of VMF stimulation on Aβ peptide induced-fibrils-formation, iii) evaluation of VMF stimulation on SH-SY5Y neuroblastoma cell line in the presence of Aβ peptide. We demonstrated for the first time that Aβ aggregation exposed to VMF during 24 h decreased ~ 86% of Aβ fibril formation compared to control. Likewise, VMF stimulation reduced Aβ fibrils-cytotoxicity and increase SH-SY5Y cell viability. These data establish the basis for future investigation that involve VMF as inhibitor of Aβ-pathology and indicate the therapeutic potential of VMF for AD treatment.

Keywords: Alzheimer’s disease; Rodin coil; Thioflavin-t assay; amyloid β plaques; magnetic stimulation.

MeSH terms

  • Amyloid beta-Peptides / chemistry*
  • Amyloid beta-Peptides / toxicity*
  • Animals
  • Cell Line, Tumor
  • Cell Survival
  • Humans
  • Magnetic Fields*
  • Mice
  • Protein Aggregates*

Substances

  • Amyloid beta-Peptides
  • Protein Aggregates