Aug. 19, 2015
Lisa Lapidus is an associate professor in the Department of Physics and Astronomy and an adjunct professor in the Department of Biochemistry and Molecular Biology. Through her research, she may be able to help deliver a knockout punch to debilitating neurodegenerative diseases, like Parkinson’s disease. She pioneered a technique using lasers to study the disease.
Developing effective treatments for neurodegenerative diseases, such as Parkinson’s disease, is one of the greatest medical challenges of the 21st century. By the time patients show symptoms and go to a doctor, aggregation already has a stronghold in their brains. In the lab, however, we can see the first steps, at the very place where the drugs could be the most effective. This could be a strong model for fighting Parkinson’s and other diseases.
We have shed light on the protein aggregation process by correlating the speed at which an unfolded protein changes shape, or reconfigures, with its tendency to clump or bind with other proteins. If reconfiguration is much faster or slower than the speed at which proteins bump into each other, aggregation is slow, but if reconfiguration is the same speed, aggregation is fast.
My lab uses lasers to study the speed of protein reconfiguration before aggregation. Proteins are chains of amino acids that do most of the work in cells. Scientists understand protein structure, but they don’t know how they are built — a process known as protein folding, which I first started researching at the National Institutes of Health.
With this technique, I have investigated a number of small molecules that interact directly with the protein and prevent aggregation by speeding up reconfiguration. Many of these molecules occur naturally — such as curcumin (from the spice turmeric) and quercetin, found in many berries and herbs — but are not viable drug candidates because they do not easily cross the blood-brain barrier, the filter that controls what chemicals reach the brain.
Another molecule, a small “molecular tweezers,” is more promising and clinical trials are being planned. We’ve also begun looking at two other proteins, the Alzheimer’s peptide and the prion protein, which is involved in Mad Cow Disease, and are seeing similar results. I’m enthusiastic about future research in this area. Physics underlies all of biology and I think understanding this connection can help prevent or cure diseases.
Came to MSU: 2004
Hometown: Bridgewater, N.J. I currently live in East Lansing with my husband and 2 sons.
Muses: The entire scientific community. If I don’t listen to them, I can’t do my job.
Favorite food: Chocolate and eggs (but not together).
Best song/group: The Beatles’ Abbey Road album (the ‘B’ side for those of a certain age).
Book I’d recommend: “Man in the High Castle” by Philip K. Dick. It’s a great piece of science fiction; read it before Amazon changes the whole thing.
Coolest gadget: iPad.
Best invention: The plow.
Worst invention: I don’t know because no one uses it.
On my bucket list: I’m too young for a bucket list.
Person I’d most like to meet (living or dead): Joss Whedon, an American screenwriter, comic book author and composer, as well as an actor and director.
Best trip/vacation: Camp Michigania, on Walloon Lake in northern Michigan near Petoskey, a University of Michigan alumni camp.
On a Saturday afternoon, you’ll likely find me: Hanging out with my kids.
Major research breakthrough of the next decade: A drug to prevent Alzheimer’s disease.
Reprinted with permission from the College of Natural Science's Classes Without Quizzes