NSF Career Award hails Blanchard's cell biology achievements

July 17, 2008 -- The National Science Foundation has given its prestigious Career Award to Weill Cornell Medical College researcher Dr. Scott Blanchard in recognition of his groundbreaking work in cell biology. The award totals more than $806,000 spread over five years.

Blanchard is perhaps best known for advancing fluorescence technologies that allow scientists to observe the activities of single-molecules in real-time. Much of his previous and ongoing research has been focused on the ribosome, the complex molecular machine responsible for translating DNA-encoded instructions into usable proteins.

"I'm extremely gratified to receive this award. It will help significantly to expand our work on the ribosome -- work that has potential for drug discovery. Nearly, half of all therapeutic agents target the ribosome. Nevertheless, we know precious little about how they affect this complex enzyme at the molecular level," Dr. Blanchard says. "The NSF award will shed important new light on conserved aspects of the ribosome mechanism across species, enhancing not only our basic knowledge how this enzyme is able to synthesize protein but also furthering our knowledge of how antibiotics work."

"It's rare that the NSF bestows such an award upon a medical college, since these grants typically go to undergraduate institutions with a heavy emphasis on the basic sciences," said Dr. David P. Hajjar, senior executive vice dean and executive vice provost of Weill Cornell Medical College. "But Weill Cornell is strongly committed to supporting basic science with an eye to translational."

Dr. Blanchard's work in fluorescence microscopy aims to revolutionize the way we examine how enzymes work.

"Until recently, scientists have been forced to observe the activity of enzymes en masse. This method measures only the average behavior of many billions of molecules present in a test tube, and is an expensive and relatively imprecise approach," Dr. Blanchard explains. "Or they rely on computational methods that animate static structural models. Single-molecule fluorescence microscopy aims to integrate these disparate views of enzyme function -- we actually watch photons of light coming out of a single molecule and use it to track a molecule's location, its interaction with other molecules, and tiny motions within the molecule itself. From these data, we hope to generate the first experimentally-validated movies of single molecules at work."

Since coming to Weill Cornell from Stanford University, Dr. Blanchard has focused his work on the ribosomal functions present in one of the most basic organisms on earth  the E. coli bacterium.

"We looked first at E. coli because it has been exhaustively researched and its basic functions are relatively well understood. It was a proof-of-principle project that demonstrated that single-molecule fluorescence microscopy could illuminate ribosomal activity," the researcher explains.

But the most exciting research lies ahead.

"We know that the ribosome works by similar mechanisms across organisms and cell types. Yet subtle variations in function are evident in the effectiveness of ribosome-targeting antibiotics used clinically for the past 50 years," Dr. Blanchard says.

These antibiotics target -- and disrupt -- bacterial ribosome functions, while leaving the human cell's ribosome alone. "We also suspect that the ribosomes of different human cell types work differently, depending on the organ or tissue in question," he adds. "Understanding and exploiting these differences may lead to opportunities for discovering highly targeted, safer and more effective medicines."

The fight against cancer is perhaps the greatest frontier for this avenue of research. "We have a pretty good idea that the ribosome functions inside cancer cells are markedly different from those inside healthy cells," Dr. Blanchard explains. "So, the ultimate goal here is to explore whether compounds like those used to target bacterial infection can be used to target only the cancer cell."

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