Vitals
Current affiliation: Virginia Tech
Age: 34
PhD alma mater: University of Florida
My lab superpower is: “I’m pretty good at quickly generating figures in Illustrator.”
My favorite TV show is: “Survivor. It’s the perfect representation of how humans work together and always a time capsule of American culture.”
Adrian Figg always wanted to be an architect. As a child, he spent hours looking up buildings on the internet and drawing floor plans on graph paper. When he took his first organic chemistry class at the University of California, Santa Barbara, he found himself captivated by architecture on the molecular scale. “It just completely clicked with the way that I think,” he says, recounting hours spent looking at drug structures on Wikipedia while working in the library.
Through his chemistry and biology classes at UCSB and a summer undergraduate research program in the Netherlands, he became drawn to polymers and proteins. He loved the idea that a relatively small number of building blocks, chained together just so, can lead to a vast array of 3D architectures and functions.
As he continued his education in polymer chemistry, Figg’s ideas for his future independent research career began to coalesce: “I really wanted a way for polymers to be able to communicate with biology,” he says.
He and his team at Virginia Tech recently showed that short polymer chains, known as oligomers, made of amino acid–inspired monomers in a random order can selectively bind to green fluorescent protein and boost its fluorescence.
Modulating proteins without precisely controlling the structure of the molecule doing the modulation seems counterintuitive according to traditional molecular-design principles. But a good approximation of the necessary chemical interactions goes a surprisingly long way, Figg says. “If you have a polymer that can squiggle around and adopt the right conformation, you’re going to get some binding interaction just statistically” with the right distribution of hydrophobic, polar, and charged groups sticking off the backbone, he explains.
These random polymers aren’t suitable as drugs, but they’re not meant to be, Figg says—though in the long term, he would like to develop polymers for treating neurodegenerative diseases. Rather, the oligomers could provide an inexpensive and scalable method for purifying proteins such as insulin or boosting selectivity in diagnostics by binding to protein impurities. “I really want to use these random heterooligomers in a directly medically relevant area,” he says.
“He’s not afraid to tackle complex problems,” says Brent S. Sumerlin, Figg’s PhD adviser at the University of Florida. As a graduate student, Figg had “an exceptionally diverse dissertation,” strongly rooted in fundamental polymer synthesis and photochemistry, Sumerlin says. And he’s now combining those skills with his postdoctoral experience on nucleic acid oligomers in Chad A. Mirkin’s group at Northwestern University in a creative and “really inspiring” way.
Figg and his team recently began collaborating with the Biomaterials, Polymers, and Advanced Constructs from Integrated Chemistry Materials Innovation Platform at UCSB to explore high-throughput methods for oligomer synthesis and protein binding. In collaboration with colleagues at Virginia Tech, they used the data to train a machine learning model. The goal, Figg says, is to be able to plug in a protein and have the model suggest polymer compositions that will either activate or inhibit it.
“We’re just learning as a society how to hijack biological systems and put them to good use, and that requires that you establish the ground rules for doing that,” Mirkin says. Figg is directly contributing to developing those design rules, which “is going to lead to, I think, a lot of really important advances,” he says.
Figg doesn’t create only random, Frank Gehry–esque polymer architectures. He and his team also make polymers with very precisely ordered block sequences, more akin to Frank Lloyd Wright on a molecular scale. They figured out a trick for controlling reversible addition–fragmentation chain transfer (RAFT) polymerization to overcome reactivity differences that had previously limited what order the monomers could go in. As a result, the polymers are tougher and stretchier.
Figg attributes his accomplishments so far to having great mentors and a dedicated group of graduate students and undergraduates working for him. He says his guiding philosophy is to lean in to what he and his team know best: polymer chemistry. “We’re not biologists. We’re not computational people. We are the polymer chemists. How do we use our expertise to ask the questions that people aren’t asking because they don’t think like us?”
