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"Peptides are a little bit like spaghetti; they're too flexible to do their jobs," said University of Illinois chemistry professor Wilfred van der Donk, who led the research with biochemistry professor Satish K. Nair. "So what nature does is it starts putting knobs in, or starts making the peptide cyclical."




Through a painstaking process of elimination, Manuel Ortega, a graduate student in van der Donk's lab, established that the amino acid glutamate was essential to nisin's transformation.

"They discovered that the dehydratase did two things," Nair said. "One is that it added glutamate (to the nisin peptide), and the second thing it did was it eliminated glutamate. But how does one enzyme have two different activities?"

To help answer this question, Yue Hao, a graduate student in Nair's lab, used X-ray crystallography to visualize how the dehydratase bound to the nisin peptide. She found that the enzyme interacted with the peptide in two ways: It grasped one part of the peptide and held it fast, while a different part of the dehydratase helped install the ring structures.

"There's a part of the nisin precursor peptide that is held steady, and there's a part that is flexible. And the flexible part is actually where the chemistry is carried out," Nair said.


"In this study, we solve a lot of questions that people have had about how dehydration works on a chemical level," van der Donk said. "And it turns out that in nature a fairly large number of natural products – many of them with therapeutic potential – are made in a similar fashion. This really is like turning on a light where it was dark before, and now we and other labs can do all kinds of things that we couldn't do previously."


Source: University of Illinois at Urbana-Champaign

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