Detection of Protein-Ligand Interactions by 19F Nuclear Magnetic Resonance Using Hyperpolarized Water. Academic Article uri icon

abstract

  • The transfer of nuclear spin hyperpolarization from water to ligand 19F spins results in a transient signal change that is indicative of protein-ligand interaction. The 19F nucleus allows for background-free detection of these signals, which are modulated by polarization transfer via pathways similar to those in a hyperpolarized 1H water LOGSY experiment. Quantification of the apparent heteronuclear cross-relaxation rates is facilitated by a simultaneous dual-channel detection of 1H and 19F signals. Calculated cross-relaxation rates for the 1H-19F transfer step indicate that these rates are sensitive to binding to medium- and large-sized proteins. The heteronuclear observation of hyperpolarization transfer from water may be used to screen protein-ligand interactions in drug discovery and other applications.

published proceedings

  • J Phys Chem Lett

altmetric score

  • 3.85

author list (cited authors)

  • Hu, J., Kim, J., & Hilty, C.

citation count

  • 2

complete list of authors

  • Hu, Jiandu||Kim, Jihyun||Hilty, Christian

publication date

  • January 2022