Researchers have designed a highly sensitive sensor capable of identifying proteins in solution down to a single molecule.

Researchers in the College of Arts and Sciences’ (A&S’) Department of Physics at Syracuse University have been studying a protein hub, called WDR5, which is responsible for many important functions within the nucleus. WDR5 has recently been heavily investigated, because it is a promising target for anti-cancer drugs. But until now, not much has been known about how WDR5 interacts transiently with other proteins inside the cell because the necessary technology to study WDR5 did not exist. Using a highly sensitive engineered biosensor, A&S researchers have uncovered new information on how WDR5 connects and disconnects with other molecules.

The collaborative project was funded through a four-year, $1.2 million Research Project Grant (R01) from the National Institutes of Health’s National Institute of General Medical Sciences (NIGMS), awarded to Liviu Movileanu, professor of physics, in 2018. The culminating results of the team’s work have been published in the journal Nature Communications. The research team also includes Lauren Ashley Mayse and Ali Imran, both graduate students in Movileanu’s lab, as well as other researchers at SUNY Upstate Medical University, Ichor Therapeutics, and the National Institutes of Health’s National Institute of Child Health and Human Development.

How it Works

The goal of the team’s study was to create an ultra-sensitive device capable of detecting and quantifying WDR5. They designed, developed, and validated a nanopore-based biosensor, which creates a tiny hole (nanopore) in a synthetic membrane and can identify proteins in solution at single-molecule precision.

The biosensor’s channel-like base creates a small hole in the synthetic membrane and allows ionic solution to flow through it. When the sensor recognizes a specific molecule, in this case WDR5, the ionic flow changes. This change in flow serves as the signal from the sensor that the targeted protein has been found.

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Materials provided by Syracuse University. Original written by Dan Bernardi. Note: Content may be edited for style and length.