Ultrafast Single-Scan 2D NMR Spectroscopic Detection of a PHIP-Hyperpolarized Protease Inhibitor

Alexey S. Kiryutin, Grit Sauer, Daniel Tietze, Martin Brodrecht, Stephan Knecht, Alexandra V. Yurkovskaya, Konstantin L. Ivanov, Olga Avrutina, Harald Kolmar, Gerd Buntkowsky

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)


Two-dimensional NMR spectroscopy is one of the most important spectroscopic tools for the investigation of biological macromolecules. However, due to the low sensitivity of NMR spectroscopy, it takes usually from several minutes to many hours to record such spectra. Here, the possibility of detecting a bioactive derivative of the sunflower trypsin inhibitor-1 (SFTI-1), a tetradecapeptide, by combining parahydrogen-induced polarization (PHIP) and ultrafast 2D NMR spectroscopy is shown. The PHIP activity of the inhibitor was achieved by labeling with O-propargyl-l-tyrosine. In 1D PHIP experiments a signal enhancement of a factor of approximately 1200 compared to standard NMR was found. This enhancement permits measurement of 2D NMR correlation spectra of low-concentrated SFTI-1 in less than 10 seconds, employing ultrafast single-scan 2D NMR detection. As experimental examples PHIP-assisted ultrafast single-scan TOCSY spectra of SFTI-1 are shown.

Original languageEnglish
Pages (from-to)4025-4030
Number of pages6
JournalChemistry - A European Journal
Issue number16
Publication statusPublished - 15 Mar 2019


  • enzyme inhibitors
  • hyperpolarization
  • parahydrogen
  • ultrafast 2D NMR
  • Magnetic Resonance Spectroscopy/methods
  • Protease Inhibitors/analysis
  • Algorithms
  • Imidazoles/chemistry
  • Tyrosine/analogs & derivatives
  • Molecular Structure
  • Peptides, Cyclic/analysis


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