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

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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

Fingerprint

Epitopes
Screening
Nuclear magnetic resonance
Galectin 1
Ligands
Epitope Mapping
Biomolecules
Lactose
Lectins
Spatial distribution
Transmitters
Magnetization
Experiments
Carbohydrates
Atoms
Molecules
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Organic Chemistry
  • Molecular Medicine
  • Molecular Biology

Cite this

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title = "15N and 13C group-selective techniques extend the scope of STD NMR detection of weak host-guest interactions and ligand screening",
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.",
keywords = "Host-guest chemistry, Molecular dynamics, Molecular recognition, NMR spectroscopy, Saturation transfer difference spectroscopy",
author = "K. K{\"o}v{\'e}r and Edit W{\'e}ber and T. Martinek and E. Monostori and G. Batta",
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TY - JOUR

T1 - 15N and 13C group-selective techniques extend the scope of STD NMR detection of weak host-guest interactions and ligand screening

AU - Kövér, K.

AU - Wéber, Edit

AU - Martinek, T.

AU - Monostori, E.

AU - Batta, G.

PY - 2010/10/18

Y1 - 2010/10/18

N2 - 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.

AB - 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.

KW - Host-guest chemistry

KW - Molecular dynamics

KW - Molecular recognition

KW - NMR spectroscopy

KW - Saturation transfer difference spectroscopy

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