Target-specific NMR detection of protein–ligand interactions with antibody-relayed 15N-group selective STD

Anasztázia Hetényi, Zsófia Hegedűs, Roberta Fajka-Boja, Éva Monostori, K. Kövér, T. Martinek

Research output: Article


Fragment-based drug design has been successfully applied to challenging targets where the detection of the weak protein–ligand interactions is a key element. 1H saturation transfer difference (STD) NMR spectroscopy is a powerful technique for this work but it requires pure homogeneous proteins as targets. Monoclonal antibody (mAb)-relayed 15N-GS STD spectroscopy has been developed to resolve the problem of protein mixtures and impure proteins. A 15N-labelled target-specific mAb is selectively irradiated and the saturation is relayed through the target to the ligand. Tests on the anti-Gal-1 mAb/Gal-1/lactose system showed that the approach is experimentally feasible in a reasonable time frame. This method allows detection and identification of binding molecules directly from a protein mixture in a multicomponent system.

Original languageEnglish
Pages (from-to)227-232
Number of pages6
JournalJournal of Biomolecular NMR
Issue number4
Publication statusPublished - dec. 1 2016


ASJC Scopus subject areas

  • Biochemistry
  • Spectroscopy

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