Luke Connal

Luke Connal

Vitals

Current affiliation: University of Melbourne (In November, he’s moving to Australian National University.)

Age: 36

Ph.D. alma mater: University of Melbourne

Advice for young scientists: “Follow your nose and make the most of your opportunities. And keep a thick skin.”

Role model: “Whoever said ‘play is the highest form of research.’ I love what I do and have fun playing with our science.”

While working as an undergrad in a polymer chemistry lab, Luke Connal realized that polymers are powerful—for example, they can be therapeutics, mining tools, or even counterfeit-proof currency.

Today, running his own lab at the University of Melbourne, Connal wants to harness the power of polymers to design catalysts that mimic enzymes. He thinks these catalytic materials could do jobs in industry or in commercial products that less-robust enzymes can’t.

“This is a platform that could really transform catalysis,” says Michelle Coote, one of Connal’s colleagues at Australian National University.

Enzymes achieve their catalytic prowess by folding in specific ways to orient key chemical groups. But when an enzyme loses this structure, it also loses its function, making the proteins sensitive to harsh conditions, such as high temperatures or high salt levels, that can unfold them.

Research at a glance

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Connal’s group designed a polymer with active sites that mimic the catalytic amino acids of proteases (left). Their polymer active sites contain the same three functional groups as the enzymes: an alcohol, an imidazole, and a carboxylate. These polymers one day could replace enzymes used in laundry detergents.
Credit: Yang H. Ku/C&EN/Shutterstock

Polymers are far more stable and can withstand a wider range of conditions. So Connal set to work on mimicking the active sites of enzymes—where the chemical action happens—in polymer structures.

His first target of mimicry was the so-called catalytic triad of proteases. These enzymes use the triad—an alcohol, a carboxylate, and an imidazole—to chew up the amide backbones of other proteins. Connal’s team earlier this year reported a polymer resin that breaks down esters with enzymelike kinetics using the same trio of functional groups.

Connal is collaborating with the consumer product company Unilever on the protease project, with the goal of replacing stain-fighting enzymes in laundry detergents with more stable, longer lasting polymers. With those applications in mind, he says his group’s goal is to keep the material’s synthesis concise and scalable.

Connal’s success is due in part to how he combines an engineer’s focus on performance with a synthetic chemist’s ability to efficiently make molecules, says Craig Hawker, Connal’s postdoc adviser at the University of California, Santa Barbara.

Besides using polymers to mimic enzymes, Connal also develops polymers for conductors in lithium-ion batteries and for purifying metals from ores. “Once you realize the potential of polymers,” he says, “there is so much you can do.”

Three key papers

Triggered and Tunable Hydrogen Sulfide Release from Photogenerated Thiobenzaldehydes” (Chem.–Eur. J. 2017, DOI: 10.1002/chem.201701206)

2D and 3D-Printing of Self-Healing Gels: Design and Extrusion of Self-Rolling Objects” (Mol. Syst. Des. Eng. 2017, DOI: 10.1039/c7me00023e)

Simple Design of an Enzyme-Inspired Supported Catalyst Based on a Catalytic Triad” (Chem 2017, DOI: 10.1016/j.chempr.2017.04.004)

Vitals

Current affiliation: University of Melbourne (In November, he’s moving to Australian National University.)

Age: 36

Ph.D. alma mater: University of Melbourne

Advice for young scientists: “Follow your nose and make the most of your opportunities. And keep a thick skin.”

Role model: “Whoever said ‘play is the highest form of research.’ I love what I do and have fun playing with our science.”

Fikile Brushett
Jillian Dempsey