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Media Credit: Conor Kevit Peter Agre won the Nobel Prize for Chemistry in 2003 while working at Hopkins.

Peter Agre looks like any other ordinary man ­- fairly tall with brown hair, dressed casually in a turtleneck - but behind his modest appearance lies a unique individual: a Nobel Prize winner dedicated to combating malaria.

A graduate from the Hopkins Medical School, Agre worked as a researcher and professor in the Department of Biological Chemistry.

In 2003, Agre won the Nobel Prize in Chemistry for his discovery of aquaporins, protein channels within the membranes of cells that allow the movement of water across the membrane.

But the discovery came as a bit of a surprise.

"It wasn't what we were looking for originally," Agre said.

"We thought that the protein we isolated was part of the Rh blood complex and, in fact, it is not. In truth, there was a little disappointment. 'Oh nuts, it is a contaminant.' But it was a pretty interesting contaminant."

When Agre matriculated to the medical school in 1970 with an interest in world health problems, much of his initial research as a student centered on cholera. After his clinical training, Agre focused much more on basic research of red blood cells, discovering the molecular basis for several diseases.

It was while investigating the molecular basis for Rh blood complex that Agre and his research team isolated the contaminating protein.

The protein contaminant turned out to be Aquaporin I, the first of 13 proteins discovered so far that are responsible for the movement of water in and out of the cell.

For a hundred years, the consensus was that water moved passively through the cell membrane without the aid of channel proteins. However, this theory did not sit well with many in the scientific community.

With the aid of other Hopkins doctors, Agre began investigating the protein.

"Once we figured out what it was, it was a great joy because we had figured out some new insight into a very long standing problem," Agre said.

When asked for a "dumbed-down" explanation of how these proteins work, Agre said, "When I was a student here, there was a wonderful faculty member here named Dan Nathans who shared the Nobel [Prize] for his discovery of restriction enzymes. And I remember distinctly an interview he had with the press. When they asked him to explain his work, and before he started they said, 'We are not scientists, we can never understand it.' He responded by saying, 'The details are complicated, but the principles are elegant and simple.' I think that is a very wise statement."

Continued...

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