Electric field for treating neurological disorders
doi:10.1038/nindia.2014.102 Published online 29 July 2014
Researchers have shown that static electric fields can be used to disintegrate fibrillar aggregates of human serum albumin, an abundant human blood protein1. This ability could potentially be used to develop an analytical tool for screening drug candidates designed to break down protein aggregates that cause neurological disorders, such as Alzheimer’s and Parkinson’s diseases.
Fibrillar protein aggregates, commonly known as amyloids, consist of misfolded proteins, and they cause various neurological, cardiovascular and arthritic diseases. Although drugs have been developed for disintegrating protein aggregates, they have relatively high toxicities.
The researchers prepared solutions of fibrillar aggregates of human serum albumin and then applied static electric fields of various strengths to them for 10 minutes. They found that the electric fields caused the human serum albumin fibrils to disintegrate.
To further probe this protein disintegration, they exposed fluorescent-dye-tagged human serum albumin to electric fields for longer durations at room temperature. After 2 hours, the fluorescence intensity of the serum albumin decreased significantly, indicating that the electric fields disintegrated the fibrillar structures of human serum albumin. The electric fields reduced the distinct beta-sheet structure of human serum albumin; the researchers attribute this to the electric fields disrupting the electrostatic interactions that hold the serum albumin fibrils together.
“This study offers a basic platform to explore the effects of electric field as a therapeutic tool,” says Sunando DasGupta, a senior author of the study. Further experiments are needed to implement controlled application of static electric field and fluorescent tagging to locate the protein fibrils in diseased patients, he adds.
1. Pandey, N. K. et al. Disruption of human serum albumin fibrils by a static electric field. J. Phys. D: Appl. Phys. 47, 305401 (2014) doi: 10.1088/0022-3727/47/30/305401