Optimization of xenon biosensors for detection of protein interactions.
Chembiochem
; 7(1): 65-73, 2006 Jan.
Article
em En
| MEDLINE
| ID: mdl-16342304
ABSTRACT
Hyperpolarized 129Xe NMR spectroscopy can detect the presence of specific low-concentration biomolecular analytes by means of a xenon biosensor that consists of a water-soluble, targeted cryptophane-A cage that encapsulates the xenon. In this work, we use the prototypical biotinylated xenon biosensor to determine the relationship between the molecular composition of the xenon biosensor and the characteristics of protein-bound resonances. The effects of diastereomer overlap, dipole-dipole coupling, chemical-shift anisotropy, xenon exchange, and biosensor conformational exchange on the protein-bound biosensor signal were assessed. It was found that an optimal protein-bound biosensor signal can be obtained by minimizing the number of biosensor diastereomers and using a flexible linker of appropriate length. Both the line width and sensitivity of chemical shift to protein binding of the xenon biosensor were found to be inversely proportional to linker length.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Xenônio
/
Técnicas Biossensoriais
/
Avidina
Tipo de estudo:
Diagnostic_studies
/
Prognostic_studies
Idioma:
En
Ano de publicação:
2006
Tipo de documento:
Article