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In 2005, Garcia and his colleagues determined the structure of IL-2, making it possible to visualize its internal features. "We thought we might be able to tilt the balance of therapeutic-to-toxic effects by modifying this protein in a way that preferentially trips off activation of a desired immune-cell type, while minimizing the activation of an unwanted cell type," he said.

For this study, Garcia's group produced a vast variety of mutated versions of the protein, and then, in a test-tube competition, compared the strength of these mutant proteins' binding to a particular cell-surface receptor, a process that is crucial to the T-cell activation needed to treat cancer. The researchers eventually obtained a mutant that Garcia dubbed "Super-2," which had more than 300 times the receptor-binding strength of natural IL-2. In subsequent tests designed to assess Super-2's ability to impede tumor growth, the new molecule outperformed natural IL-2 by a significant margin.

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