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The axial and equatorial protons in cyclohexane can be distinguished by performing a variable-temperature NMR experiment. In this process, except for one proton, the remaining eleven protons are replaced by deuterium. The deuterium substitution avoids the possible peak splitting caused by the spin-spin coupling between the adjacent protons. The remaining proton flips between the axial and equatorial positions.
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Nuclear magnetic resonance (NMR) spectroscopy is a very valuable analytical technique for researchers. It has been used for more than 50 years as an analytical tool. F. Bloch and E. Purcell formulated NMR in 1946 and won the 1952 Nobel Prize in Physics  for their work. Biological macromolecules such as proteins, nucleic acids, lipids, and organic molecules including pharmaceutical compounds, can be studied using this versatile tool that exploits the magnetic properties of certain nuclei.
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The Pople nomenclature system classifies spin systems based on the difference between their chemical shifts. Coupled spins are denoted by capital letters with subscripts indicating the number of equivalent nuclei. When the coupled nuclei have well-separated chemical shifts, they are assigned letters that are far apart in the alphabet, such as A and X. When the difference in chemical shifts is small, coupled nuclei are named using adjacent letters of the alphabet (AB, MN, or XY).
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Cryptophane Nanoscale Assemblies Expand 129Xe NMR Biosensing.

Serge D Zemerov1, Benjamin W Roose1, Mara L Greenberg1

  • 1Department of Chemistry , University of Pennsylvania , 231 S 34th St. , Philadelphia , Pennsylvania 19104 , United States.

Analytical Chemistry
|May 22, 2018
PubMed
Summary

Cryptophane biosensors detect targets using xenon NMR. Monomeric solutions enhance detection sensitivity, but biosensor disaggregation influences signal interpretation, requiring data reevaluation for improved accuracy.

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Area of Science:

  • Biomedical Engineering
  • Chemical Biology
  • Nuclear Magnetic Resonance Spectroscopy

Background:

  • Cryptophane-based biosensors show promise for ultrasensitive detection of biomedical targets using 129Xe NMR.
  • Understanding cryptophane aggregation and solution behavior is crucial for optimizing biosensor performance.

Purpose of the Study:

  • To investigate the aggregation state and solution behavior of cryptophane biosensors.
  • To explore the role of stoichiometry and disaggregation in cryptophane-based biosensing of carbonic anhydrase isozymes.
  • To determine optimal conditions for ultrasensitive detection using hyper-CEST NMR.

Main Methods:

  • Dynamic light scattering to assess cryptophane aggregate size.
  • Acridine orange fluorescence quenching assays to quantify aggregation.
  • Hyper-CEST NMR spectroscopy to detect carbonic anhydrase isozymes (CAII and CAXII).

Main Results:

  • Cryptophanes form water-soluble aggregates (10-100 nm) with critical concentrations between 200-600 nM.
  • Cryptophane biosensor C8B disaggregated upon binding carbonic anhydrase (CA), forming a 1:1 complex.
  • C8B exhibited higher affinity for CAII than CAXII; however, biosensor disaggregation contributed to the observed 129Xe NMR chemical shift changes.
  • Monomeric cryptophane solutions improved hyper-CEST saturation contrast for ultrasensitive detection.

Conclusions:

  • Monomeric cryptophane solutions enhance hyper-CEST contrast, enabling ultrasensitive detection of biosensor-protein complexes.
  • Biosensor disaggregation significantly impacts 129Xe NMR signals, necessitating reinterpretation of previous data.
  • These findings provide critical insights for advancing cryptophane-based xenon biosensors.