nently in disease as well as in normal development, Roberts said.
It is the most targeted family of receptors by drug manufacturers, Roberts said, estimating that a quarter of all pharmaceuticals focus on GPCRs.
This approach should be generally applicable, he added.
And generally powerful, given that GPCRs are extremely unstable and difficult to work with. The Roberts group went around the problem by disconnecting the unstable part of the receptor and running experiments only on the part of the receptor that sticks out of the cell.
Though there were no guarantees that inhibiting one part of the receptor would harm the whole, the strategy succeeded.
Roberts method builds on his co-discovery, in 1997, of a simple method for building libraries of trillions of short proteins, or peptides.
In the new study, Roberts and his group literally threw trillions of peptides at the receptor and saved the ones that stuck.
We let the molecules themselves decide if they bind, rather than trying to design them rationally, he said.
After multiple cycles, the researchers had a group of peptides that fixed to the receptor and not to any other protein.
Fruit flies genetically transformed to produce such peptides lived longer, suggesting that the peptides were interfering with the receptors normal function.
However the questions that have been left unanswered are why these particular peptides work, and why the receptor they target plays such an important role in fruit fly aging.
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