15N and 13C group-selective techniques extend the scope of STD NMR detection of weak host-guest interactions and ligand screening

Research output: Article

7 Citations (Scopus)

Abstract

Saturation transfer difference (STD) is a valuable tool for studying the binding of small molecules to large biomolecules and for obtaining detailed information on the binding epitopes. Here, we demonstrate that the proposed 15N/13C variants of group-selective, "GS-STD" experiments provide a powerful approach to mapping the binding epitope of a ligand even in the absence of efficient spin diffusion within the target protein. Therefore, these experimental variants broaden the scope of STD studies to smaller and/or more-dynamic targets. The STD spectra obtained in four different experimental setups (selective 1H STD, 15N GS-STD, 13CAr and 13Caliphatic GS-STD approaches) revealed that the signal-intensity pattern of the difference spectra is affected by both the type and the spatial distribution of the excited "transmitter" atoms, as well as by the efficiency of the spin-diffusion-mediated magnetization transfer. The performance of the experiments is demonstrated on a system by using the lectin, galectin-1 and its carbohydrate ligand, lactose.

Original languageEnglish
Pages (from-to)2182-2187
Number of pages6
JournalChemBioChem
Volume11
Issue number15
DOIs
Publication statusPublished - okt. 18 2010

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Organic Chemistry

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