Three Evolutionary Scientists Share This Year’s Nobel Prize in Chemistry

Frances Arnold, George Smith and Gregory Winter employed principles seen in evolution to develop proteins that tackle global chemical problems

From L to R: Frances H. Arnold was recognized for her work in the directed evolution of enzymes, while George P. Smith and Sir Gregory Winter were honored for the phage display of peptides and antibodies Courtesy of Niklas Elmehed/Royal Swedish Academy of Sciences

This year’s Nobel Prize in Chemistry was awarded to three researchers whose pioneering work with proteins has, in the words of one committee member, “applied the principles of Darwin in the test tube.”

Frances H. Arnold of the California Institute of Technology—only the fifth female Nobel Laureate in the chemistry prize’s 117-year history—was recognized for conducting the first directed evolution of enzymes, or catalysts that enable the production of chemical substances, such as environmentally-friendly pharmaceuticals and biofuels. George P. Smith of the University of Missouri and Sir Gregory P. Winter of the MRC Laboratory of Molecular Biology in Cambridge were jointly honored for their contributions to the phage display method, which can be used to evolve new proteins and produce powerful pharmaceuticals.

Arnold will take home half of the roughly $1.01 million prize money, while Smith and Winter will split the remaining funds.

According to a statement released by the Royal Swedish Academy of Sciences, which is responsible for nominating and selecting the Nobel Laureates in Physics and Chemistry, the three honorees “have been inspired by the power of evolution and used the same principles—genetic change and selection—to develop proteins that solve mankind’s chemical problems.”

The Guardian’s Nicola Davis reports that Arnold’s directed evolution of enzymes (proteins that catalyze, or accelerate, chemical reactions) essentially boils down to the introduction of genetic mutations that allow enzymes to perform more efficiently or in ways that they normally wouldn’t.

This process is inspired by evolution: As Charles Darwin theorized, organisms with advantageous traits tend to have more offspring and eventually trigger natural selection, which favors those equipped for survival and reproduction over those less suited to their environment. In Arnold’s experiments, these advantageous traits equate to mutated enzymes that exhibit high levels of efficiency and can replace strong solvents, heavy metals and corrosive acids in the production of pharmaceuticals, plastics and other chemicals.

Arnold’s work has placed her at the forefront of enzyme research. The Royal Swedish Academy notes that the catalysts produced in her lab can produce materials that don’t yet exist in nature, speed up chemical reactions, produce fewer by-products and, in certain cases, replace the heavy metals typically used in traditional chemistry. Currently, her main area of focus is the production of renewable energy, with a long-term goal of creating environmentally-friendly fuel that will revolutionize the transportation sector.

“Twenty-five years ago, [this technology] was considered the lunatic fringe,” Arnold explained in a 2014 interview marking her induction to the National Inventors Hall of Fame. “Scientists didn’t do that. Gentlemen didn’t do that. But since I’m an engineer and not a gentleman, I had no problem with that.”

As only the fifth woman out of more than 178 honorees to receive the chemistry prize, Arnold's win is significant. Only 3 percent of science prizes have been awarded to women in science, Erin Ross reported for Axios last year. Women scientists have historically been snubbed by the Nobel committee. The third woman to ever to receive the physics prize was awarded yesterday.

This year’s other honorees—Smith and Winter—have both made significant contributions to the phage display method, which finds a bacteria-infecting virus known as a bacteriophage employed in the evolution of new proteins. Smith developed the process in 1985, and Winter built on his research to conduct the directed evolution of antibodies and, subsequently, production of new pharmaceuticals.

According to a Royal Swedish Academy statement, Smith knew it was possible to manipulate a phage’s (virus that infects bacteria) genetic material and change the molecules coating its surface, so he decided to use the virus as a means of identifying an unknown gene for a known protein, and vice versa. As The Guardian’s Davis explains, once Smith inserted a specific gene into a phage, he could identify the protein that emerged on its surface and gain a better understanding of the relationship between certain genes and proteins.

Winter’s research relies on phase display for the directed evolution of antibodies, or Y-shaped proteins that attach to infectious viruses and bacteria and let immune cells know they need to ward off an attempted invasion. During the 1990s, he and his colleagues set out to design pharmaceuticals that acted like antibodies to block specific ailments, and by 2002, they had created an antibody-inspired pharmaceutical that was officially approved for the treatment of rheumatoid arthritis. Today, phage display of antibodies can be used to treat diseases as varied as metastatic cancer, inflammatory bowel diseases and anthrax poisoning.

“Pretty much every Nobel laureate understands that what he’s getting the prize for is built on many precedents, a great number of ideas and research that he is exploiting because he is at the right place at the right time,” Smith said in an early morning interview with the Associated Press.

He concludes, “Very few research breakthroughs are novel. Virtually all of them build on what went on before. It’s happenstance. That was certainly the case with my work. Mine was an idea in a line of research that built very naturally on the lines of research that went before.”

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