Health
Nanopore-based sensing devices can provide volumetric information on tau and tubulin proteins
Tau and tubulin proteins are one of the main causes of many neurodegenerative diseases such as Alzheimer’s disease and Parkinson’s disease. Most of the progression of neurodegenerative diseases is associated with aggregation of these proteins in the brain.
Inspired by one of her PhD students who wanted to study tau and tubulin proteins, University of Arkansas physics professor Jiali Li and her group developed a special silicon nitride nanopore-based created a sensing device for
of Journal of Applied Physics, AIP Publishing, Acharjee et al. We present a device designed to provide volumetric information about tau and tubulin protein molecules and their aggregation states at the single-molecule level within their native environment.
To create the sensor, the team investigated how proteins change the current and voltage flowing through the nanopore system.
Ohm’s law is the underlying physics that enables nanopore devices to sense protein molecules. Tiny holes -; 6 to 30 nanometers -; made of thin silicon nitride films and supported by a silicon substrate. When it is placed in a solution containing salt ions, applying a voltage drives the flow of ions through the hole or nanopore. This creates an ionic current in the open pores. ”
Jiali Li, Professor of Physics, University of Arkansas
For charged protein molecules – often thousands of times larger than ions – when in close proximity to the nanopore, they are pushed into the nanopore and block the flow of some ions. This reduces the open pore current.
“The amount of current drop produced by a protein molecule is proportional to the volume or size and shape of the protein,” said Li. “This means that when protein A binds to protein B, it produces a current drop proportional to the volume of A+B, and aggregated protein A causes a current drop about several times higher.”
This will allow Li and her group to investigate protein binding and aggregation within the nanopore device. The residence time of a protein in a nanopore is inversely proportional to its charge and also provides useful information about protein molecules.
“Our study shows that silicon nitride nanopore devices can measure the volumetric information of tau and tubulin protein molecules and their aggregation under different biological conditions. A better understanding of the aggregation process will also enable the development of drugs and other therapeutics to treat neurodegenerative diseases,” said Li.
Using their solid-state nanopore device along with other nanotechnology tools, “we plan to systematically study the mechanisms of protein aggregation under different biological conditions, such as temperature, pH and salt concentration,” she says. Told.
sauce:
Journal reference:
ACCHARGE, MC, and others. (2023) Protein aggregation characterization of tau and tubulin by solid-state nanopore method and atomic force microscopy. Applied Physics Journal. doi.org/10.1063/5.0123688.
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