Optimization of Xenon Biosensors for Detection of ProteinInteractions Page: 4 of 44
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region uses a molecular adaptor, termed a xenon biosensor. This
sensor was developed as a means to "functionalize" polarized
xenon in aqueous solutions and target it to report on a specific
biomolecular target or event. The prototypical xenon biosensor
consists of three parts, a xenon-binding cryptophane-A cage, a
short peptide for water solubility, and a moiety that binds a
specific biomolecule. A biotinylated sensor was used to
demonstrate that the biosensor-bound xenon resonances
significantly broaden and shift downfield in the presence of
avidin. -6 The sensitivity of biosensor-encapsulated xenon to
its local environment indicates that "functionalized" xenon can
serve as a magnetic resonance reporter for targeted in situ
biosensing and imaging.[7
Our initial biotinylated cryptophane-A construct (Scheme 1,
1) gave rise to four narrow 129Xe resonances when free in
solution. These four resonances derive from the four
diastereomers RLL, RLR, LLL, and LLR that arise from the
chirality of the three biosensor components, the cage, peptide,
and maleimide.Y In the absence of protein, two of the
diastereomer resonances almost completely overlap with the other
two, yielding two slightly separated peaks of 20 Hz total
linewidth. The avidin-bound form of 1 yielded a single broad
peak -200 Hz in linewidth that was shifted -2 ppm downfield4
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Lowery, Thomas J.; Garcia, Sandra; Chavez, Lana; Ruiz, E.Janette; Wu, Tom; Brotin, Thierry et al. Optimization of Xenon Biosensors for Detection of ProteinInteractions, article, August 3, 2005; Berkeley, California. (https://digital.library.unt.edu/ark:/67531/metadc874103/m1/4/: accessed April 25, 2024), University of North Texas Libraries, UNT Digital Library, https://digital.library.unt.edu; crediting UNT Libraries Government Documents Department.