New method simplifies the search for protein receptor complexes, speeding drug development

phys.org | 7/26/2018 | Staff
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For a drug to intervene in cells or entire organs that are not behaving normally it must first bind to specific protein receptors in the cell membranes. Receptors can change their molecular structure in a multitude of ways during binding—and only the right structure will "unlock" the drug's therapeutic effect.

Now, a new method of assessing the actions of medicines by matching them to their unique protein receptors has the potential to greatly accelerate drug development and diminish the number of drug trials that fail during clinical trials.

Method - Research - Teams - University - Wisconsin-Milwaukee

The method, developed by research teams from the University of Wisconsin-Milwaukee and the University of Glasgow, reduces the time and labor of finding the protein receptors "with the right response" to drug candidates by several orders of magnitude.

"It opens up a huge playing field for finding drug targets and drug stratification," said Valerica Raicu, UW-Milwaukee professor of physics. "Using this method, we can characterize how each receptor responds differently to various drug candidates."

Study - Today - Nature - Methods

The study appears today in the journal Nature Methods.

The researchers' method tracks a chemical process called oligomerization that occurs when a receptor exists as a single subunit, but then shifts to a multi-structure—an oligomer—in the presence of the ligand (drug compound), or vice versa.

Receptors - Raicu - Author - Paper - Compound

"We used to think of these receptors as binary," said Raicu, who is lead author on the paper. "They were either activated by the compound or not. But now we are beginning to understand that, depending on the ligand, the same receptor can produce many different responses."

The researchers first tested the method using fused florescent proteins produced by UW-Milwaukee assistant professor Ionel Popa. Then they validated the method on a receptor for a growth factor where malfunction is often linked to cancer—the epidermal growth factor receptor (EGF)....
(Excerpt) Read more at: phys.org
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