Xenon ‘Cage' Is a Novel Approach to Studying Changes in Protein Structure

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Restricting xenon atoms in cages may ironically liberate drug discovery research to tackle new problems in the future, according to UC Berkeley researchers.

UC Berkeley chemistry professors Alexander Pines and David Wemmer, in collaboration with the Scripps Research Institute, have developed biosensors based on the element xenon that are capable of detecting and distinguishing protein conformations.

Many proteins are not capable of interacting with xenon. Placing the atom in a molecular cage provides a convenient handle for proteins to grasp, allowing the benefits of the technique to be generalized for a variety of biological systems.

The method may pave the way for the detection of small molecule ligand protein interactions and protein-protein interactions, said graduate student Seth Rubin, a member of Wemmer's research group.

The approach relies upon a common technique of chemical analysis known as nuclear magnetic resonance (NMR), which is capable of determining the structure of complex molecules.

NMR involves magnetically perturbing molecules and watching their transitions back to a resting state.

The process is analogous to quickly pushing an object up a hill and carefully observing its rapid descent-by watching how the object tumbled down, conclusions can be made about its shape.

When the UC Berkeley researchers examined xenon magnetic resonance signals produced from a mixture of xenon and proteins, they were able to distinguish the minute differences between protein conformations.

NMR is notorious for producing weak signals, but the use of xenon allowed for improved detection of protein structure.

Such studies can be made very specific when ligands of interest are attached to the xenon cages.

Quantifying how much of a certain molecule is contained in a mixture, is one possible application of the research and is important when it comes to treating diseases like diabetes.

"You might just want to quantify how much glucose there is in a solution," Rubin said. "And you can do that by having a protein that interacts with that glucose and detecting that interaction."

This discovery may also aid drug discovery efforts, as pharmaceutical research usually focuses on small molecules and their interactions with proteins.

"If you're developing a drug, usually, what you do is you have some sort of lead compound that you think will interact with the protein," Rubin said. "And then what you do is you can make a whole library of compounds that in some way look like the initial lead but with slight modification. The idea is that you want to screen these very rapidly to see if they react with proteins."

Although the project still remains in preliminary stages of development, the scientists remain optimistic about the ability of the research to eventually lead the way for further advances in biological sensory techniques.

The research may also impact the field of medicine by improving magnetic resonance imaging (MRI).

"Nuclear magnetic resonance and MRI are basically the same technique, utilizing the same physics," Pelton said. "Thus, it should be reasonably straightforward to employ MRI in combination with the new biosensor to actual clinical situations, although that is still a ways off."


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