Before Nicolas Fawzi could begin making discoveries about the physical behavior of proteins, he had to rediscover that he wanted to be a scientist at all.
Fawzi was interested in science as a kid, particularly astrophysics. He was closer to his eventual ambition when he enrolled in a dual degree program as an undergrad at the University of Pennsylvania, studying business with a concentration in marketing from the Wharton School and bioengineering. At the time, thinking practically, he figured he’d carve out a career in business development at a biotech company, but as sometimes happens with some double majors, one discipline exerted a stronger pull than the other.
“I realized after interning for a summer working in small business development that my passion was for science and if I was to focus on business, I would miss the science,” he said. “That’s where my curiosity was.”
So Fawzi went to graduate school at the University of California–Berkeley (jointly with University of California–San Francisco). He earned his Ph.D. in 2007 and took a postdoctoral position at the National Institutes of Health. He emerged an accomplished young expert on detecting and modeling the molecular structure of the harmful plaques of clumped-up protein fibers implicated in Alzheimer’s disease, type 2 diabete,s and other serious medical problems. This month he’ll begin his Brown career as assistant professor in the Department of Molecular Pharmacology, Physiology, and Biotechnology.
A particularly notable line on this newcomer’s CV is his lead authorship on a study in the top journal Nature in October 2011. In that work, Fawzi and his co-authors managed to capture with atomic resolution the binding interaction of a small individual protein called a peptide with one of those protein clumps, a dynamic that no one had been able to capture previously. A key insight was to apply a computer model to the data produced by an imaging technique called nuclear magnetic resonance (NMR) spectroscopy to turn raw data into a detailed picture of the structure and motions in the aggregates.
At Brown, Fawzi hopes to continue developing techniques that combine computer models and NMR in the hope of precisely characterizing the plaques, more technically known as protein aggregates or “fibrillar macromolecular systems.” In order to defeat them, scientists need to resolve not only their structure, but also how they disrupt cell membranes and receptors to cause disease. When that’s done well enough, scientists will have the means to determine how to break up the aggregates or how to interfere with the harmful interactions they inflict on brain cells in the case of Alzheimer’s disease and pancreatic cells in the case of diabetes.
An improved understanding of the structure of molecular protein fibers, Fawzi added, could also shed light on new targets for antibiotics and how cancer cells separate from tumors and spread.
Fawzi decided to pursue this work at Brown because he sees opportunities for collaboration among scientists in a wide variety of scientific and medical fields. At the same time, he’s encouraged by the University’s significant emphasis in the field that’s particularly near and dear to him.
“The administration is excited about structural biology,” he said. “It’s a growing field at Brown.”
In addition to some hiring, another sign of the excitement is that the University recently acquired a new 850 MHz NMR spectrometer, to be located in the newly established Structural Biology Core Facility, with a world-class, amazingly strong 20-Tesla magnet.
Fawzi is also excited to teach. After all, it was the guidance of professors and mentors at Penn, Cal, and NIH that helped him commit to and clarify his career as a scientist rather than a biotech businessman.
“Their investment in my education motivated me to be come a professor,” he said.
And as a former business student, he still knows a thing or two about the value of a good investment.