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Report: Proteins can be engineered as widely adaptable 'bioelectronic' sensors

ing of blood glucose in people with diabetes and could also provide a long-term sensor as the basis for an artificial pancreas.

In other applications, Hellinga foresees use of the biosensors to monitor pollutants and chemical and bio-warfare agents. He emphasized the adaptability of the system. "These engineered proteins are based on proteins that bacteria use to sense their chemical environment, and since there are perhaps hundreds or thousands that exist, they provide a basis for a vast array of chemical sensors," Hellinga said. "Using powerful computational design tools that we have developed, it is possible to engineer these candidates to dramatically alter their specificity and sensitivity."

In contrast, said Hellinga, other approaches to biosensors are more complex and less robust, depending on enzymatic reactions that involve measuring the output of chemical reactions and replenishing consumed chemicals. Also, such biosensors have largely depended on natural proteins, limiting their adaptability. "Our engineered proteins can be thought of as solid-state entities that include both a biological component and an electronic component," he said

In the Science paper, Hellinga and his colleagues described how they started with natural bacterial proteins called "bacterial periplasmic binding proteins." These proteins constitute a large "superfamily" of proteins on the bacterial surface that the organisms use to sense food sources such as sugars and to avoid toxic chemicals.

Besides their broad variability, the major advantage of such proteins is that the protein's chemical-sensing active site is "allosterically" coupled to the domain that sends a signal to the bacterial metabolic pathways. Such internal signals trigger actions such as moving toward a food source. Allosteric coupling means that the two domains are separated on the protein, and thus one can be altered even drastically without affecting the other. In particular, the bacteria
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Contact: Monte Basgall
monte.basgall@duke.edu
919-681-8057
Duke University
30-Aug-2001


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