Ligand based NMR methods for drug discovery

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Ligand based NMR methods for drug discovery. / Ludwig, Christian; Gunther, Ulrich.

In: Frontiers in Bioscience, Vol. 14, 01.01.2009, p. 4565-74.

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@article{4ad4dbc0121842069b56997e371a7e54,
title = "Ligand based NMR methods for drug discovery",
abstract = "NMR has a long history in drug discovery and hit-to-lead optimization. Compared to many other methods NMR has the advantage of combining structural and functional parameters to characterize protein inhibitor interactions. NMR methods used in this context can be split into two categories; protein based experiments using isotopically labelled protein samples and a broad range of ligand based methods. Recently, there has been a strong emphasis on so-called ligand-based methods which offer a broad range of options to determine binding epitopes. Ligand-based methods are attractive because they are broadly applicable, impose few constraints on the composition of the target protein and don't require isotopic labeling of the protein or ligands. Such experiments include diffusion experiments, saturation transfer difference (STD-NMR), NOE pumping, waterLOGSY, SALMON, transferred-NOE and INPHARMA. Ligand-based NMR methods have been employed in screening and in lead optimization. One key advantage arises from their capability to pick up specific interactions for compounds of relatively low affinity and their ability to provide limited structural information without any need of crystallization or isotopic labeling.",
keywords = "Bioaffinity Study, Small Molecule Screening, High-throughput screening, Protein Relaxation, Protein Binding Sites, Structure Activity Relationship, Review, Drug-Protein Interactions",
author = "Christian Ludwig and Ulrich Gunther",
year = "2009",
month = jan,
day = "1",
doi = "10.2741/3549",
language = "English",
volume = "14",
pages = "4565--74",
journal = "Frontiers in Bioscience",
issn = "1093-9946",
publisher = "Frontiers in Bioscience",

}

RIS

TY - JOUR

T1 - Ligand based NMR methods for drug discovery

AU - Ludwig, Christian

AU - Gunther, Ulrich

PY - 2009/1/1

Y1 - 2009/1/1

N2 - NMR has a long history in drug discovery and hit-to-lead optimization. Compared to many other methods NMR has the advantage of combining structural and functional parameters to characterize protein inhibitor interactions. NMR methods used in this context can be split into two categories; protein based experiments using isotopically labelled protein samples and a broad range of ligand based methods. Recently, there has been a strong emphasis on so-called ligand-based methods which offer a broad range of options to determine binding epitopes. Ligand-based methods are attractive because they are broadly applicable, impose few constraints on the composition of the target protein and don't require isotopic labeling of the protein or ligands. Such experiments include diffusion experiments, saturation transfer difference (STD-NMR), NOE pumping, waterLOGSY, SALMON, transferred-NOE and INPHARMA. Ligand-based NMR methods have been employed in screening and in lead optimization. One key advantage arises from their capability to pick up specific interactions for compounds of relatively low affinity and their ability to provide limited structural information without any need of crystallization or isotopic labeling.

AB - NMR has a long history in drug discovery and hit-to-lead optimization. Compared to many other methods NMR has the advantage of combining structural and functional parameters to characterize protein inhibitor interactions. NMR methods used in this context can be split into two categories; protein based experiments using isotopically labelled protein samples and a broad range of ligand based methods. Recently, there has been a strong emphasis on so-called ligand-based methods which offer a broad range of options to determine binding epitopes. Ligand-based methods are attractive because they are broadly applicable, impose few constraints on the composition of the target protein and don't require isotopic labeling of the protein or ligands. Such experiments include diffusion experiments, saturation transfer difference (STD-NMR), NOE pumping, waterLOGSY, SALMON, transferred-NOE and INPHARMA. Ligand-based NMR methods have been employed in screening and in lead optimization. One key advantage arises from their capability to pick up specific interactions for compounds of relatively low affinity and their ability to provide limited structural information without any need of crystallization or isotopic labeling.

KW - Bioaffinity Study

KW - Small Molecule Screening

KW - High-throughput screening

KW - Protein Relaxation

KW - Protein Binding Sites

KW - Structure Activity Relationship

KW - Review

KW - Drug-Protein Interactions

U2 - 10.2741/3549

DO - 10.2741/3549

M3 - Article

C2 - 19273371

VL - 14

SP - 4565

EP - 4574

JO - Frontiers in Bioscience

JF - Frontiers in Bioscience

SN - 1093-9946

ER -