RESUMO
We employed dielectrophoresis to a yeast cell suspension containing amyloid-beta proteins (Aß) in a microfluidic environment. The Aß was separated from the cells and characterized using the gradual dissolution of Aß as a function of the applied dielectrophoretic parameters. We established the gradual dissolution of Aß under specific dielectrophoretic parameters. Further, Aß in the fibril form at the tip of the electrode dissolved at high frequency. This was perhaps due to the conductivity of the suspending medium changing according to the frequency, which resulted in a higher temperature at the tips of the electrodes, and consequently in the breakdown of the hydrogen bonds. However, those shaped as spheroidal monomers experienced a delay in the Aß fibril transformation process. Yeast cells exposed to relatively low temperatures at the base of the electrode did not experience a positive or negative change in viability. The DEP microfluidic platform incorporating the integrated microtip electrode array was able to selectively manipulate the yeast cells and dissolve the Aß to a controlled extent. We demonstrate suitable dielectrophoretic parameters to induce such manipulation, which is highly relevant for Aß-related colloidal microfluidic research and could be applied to Alzheimer's research in the future.