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Structure of a 129Xe-cryptophane biosensor complexed with human carbonic anhydrase II.

ABSTRACT: Cryptophanes represent an exciting class of xenon-encapsulating molecules that can be exploited as probes for nuclear magnetic resonance imaging. The 1.70 A resolution crystal structure of a cryptophane-derivatized benezenesulfonamide complexed with human carbonic anhydrase II shows how an encapsulated xenon atom can be directed to a specific biological target. The crystal structure confirms binding measurements indicating that the cryptophane cage does not strongly interact with the surface of the protein, which may enhance the sensitivity of 129Xe NMR spectroscopic measurements in solution.

SUBMITTER: Aaron JA

PROVIDER: S-EPMC2408383 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature

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Structure of a 129Xe-cryptophane biosensor complexed with human carbonic anhydrase II.

Aaron Julie A JA Chambers Jennifer M JM Jude Kevin M KM Di Costanzo Luigi L Dmochowski Ivan J IJ Christianson David W DW

Journal of the American Chemical Society 20080508 22

Cryptophanes represent an exciting class of xenon-encapsulating molecules that can be exploited as probes for nuclear magnetic resonance imaging. The 1.70 A resolution crystal structure of a cryptophane-derivatized benezenesulfonamide complexed with human carbonic anhydrase II shows how an encapsulated xenon atom can be directed to a specific biological target. The crystal structure confirms binding measurements indicating that the cryptophane cage does not strongly interact with the surface of ...[more]

PMID: 18461940

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