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A new look at proteins in living cells
Date:8/28/2012

Proteins adorning the surfaces of human cells perform an array of essential functions, including cell signaling, communication and the transport of vital substances into and out of cells. They are critical targets for drug delivery and many proteins are now being identified as disease biomarkers early warning beacons announcing the pre-symptomatic presence of cancers and other diseases.

While study of the binding properties of membrane proteins is essential, detailed analysis of these complex entities is tricky. Now, Nongjian (NJ) Tao, Professor of Electrical Engineering, and director of the Center for Bioelectronics and Biosensors at Arizona State University's Biodesign Institute has devised a new technique for examining the binding kinetics of membrane proteins.

"This is a very important but very difficult problem to solve," Tao notes. "We demonstrate a new method of approaching the issue, which provides a quantitative analysis of protein interactions on the surface of a cell."

The technique known as SPR microscopy holds the potential to simplify the study of membrane proteins, thereby streamlining the development of new drugs, aiding the identification of diagnostic biomarkers and improving the understanding of cell-pathogen interactions.

The group's results appear in this week's advanced online issue of the journal Nature Chemistry.

Typically, proteins attached to or embedded in the cell membrane's lipid bilayer are either tagged with fluorescent markers or extracted from their locations, purified and immobilized on a glass surface in protein microarrays. These efforts may not accurately reflect native configuration and function.

Membrane proteins are complex structures whose subtle performance is often related to alterations in conformation and the particular binding kinetics at work. Existing techniques using florescent markers have been applied to pinpoint binding events, but these only perm
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Contact: Joseph Caspermeyer
Joseph.Caspermeyer@asu.edu
Arizona State University
Source:Eurekalert  

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