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1D NMR WaterLOGSY as an efficient method for fragment-based lead discovery

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1D NMR WaterLOGSY as an efficient method for fragment-based lead discovery. / Raingeval, Claire; Cala, Olivier; Brion, Béatrice; Le Borgne, Marc; Hubbard, Roderick Eliot; Krimm, Isabelle.

In: JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, Vol. 34, No. 1, 09.07.2019, p. 1218-1225.

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Harvard

Raingeval, C, Cala, O, Brion, B, Le Borgne, M, Hubbard, RE & Krimm, I 2019, '1D NMR WaterLOGSY as an efficient method for fragment-based lead discovery', JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, vol. 34, no. 1, pp. 1218-1225. https://doi.org/10.1080/14756366.2019.1636235

APA

Raingeval, C., Cala, O., Brion, B., Le Borgne, M., Hubbard, R. E., & Krimm, I. (2019). 1D NMR WaterLOGSY as an efficient method for fragment-based lead discovery. JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, 34(1), 1218-1225. https://doi.org/10.1080/14756366.2019.1636235

Vancouver

Raingeval C, Cala O, Brion B, Le Borgne M, Hubbard RE, Krimm I. 1D NMR WaterLOGSY as an efficient method for fragment-based lead discovery. JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY. 2019 Jul 9;34(1):1218-1225. https://doi.org/10.1080/14756366.2019.1636235

Author

Raingeval, Claire ; Cala, Olivier ; Brion, Béatrice ; Le Borgne, Marc ; Hubbard, Roderick Eliot ; Krimm, Isabelle. / 1D NMR WaterLOGSY as an efficient method for fragment-based lead discovery. In: JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY. 2019 ; Vol. 34, No. 1. pp. 1218-1225.

Bibtex - Download

@article{3d85f2f496284793a7fd80f76b2dfe56,
title = "1D NMR WaterLOGSY as an efficient method for fragment-based lead discovery",
abstract = "WaterLOGSY is a sensitive ligand-observed NMR experiment for detection of interaction between a ligand and a protein and is now well-established as a screening technique for fragment-based lead discovery. Here we develop and assess a protocol to derive ligand epitope mapping from WaterLOGSY data and demonstrate its general applicability in studies of fragment-sized ligands binding to six different proteins (glycogen phosphorylase, protein peroxiredoxin 5, Bcl-xL, Mcl-1, HSP90, and human serum albumin). We compare the WaterLOGSY results to those obtained from the more widely used saturation transfer difference experiments and to the 3D structures of the complexes when available. In addition, we evaluate the impact of ligand labile protons on the WaterLOGSY data. Our results demonstrate that the WaterLOGSY experiment can be used as an additional confirmation of the binding mode of a ligand to a protein.",
keywords = "binding mode, fragment-based lead discovery, saturation transfer difference, solvent-exposed, WaterLOGSY",
author = "Claire Raingeval and Olivier Cala and B{\'e}atrice Brion and {Le Borgne}, Marc and Hubbard, {Roderick Eliot} and Isabelle Krimm",
note = "{\textcopyright} 2019 The Author(s).",
year = "2019",
month = jul,
day = "9",
doi = "10.1080/14756366.2019.1636235",
language = "English",
volume = "34",
pages = "1218--1225",
journal = "JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY",
issn = "1475-6366",
publisher = "Informa Healthcare",
number = "1",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - 1D NMR WaterLOGSY as an efficient method for fragment-based lead discovery

AU - Raingeval, Claire

AU - Cala, Olivier

AU - Brion, Béatrice

AU - Le Borgne, Marc

AU - Hubbard, Roderick Eliot

AU - Krimm, Isabelle

N1 - © 2019 The Author(s).

PY - 2019/7/9

Y1 - 2019/7/9

N2 - WaterLOGSY is a sensitive ligand-observed NMR experiment for detection of interaction between a ligand and a protein and is now well-established as a screening technique for fragment-based lead discovery. Here we develop and assess a protocol to derive ligand epitope mapping from WaterLOGSY data and demonstrate its general applicability in studies of fragment-sized ligands binding to six different proteins (glycogen phosphorylase, protein peroxiredoxin 5, Bcl-xL, Mcl-1, HSP90, and human serum albumin). We compare the WaterLOGSY results to those obtained from the more widely used saturation transfer difference experiments and to the 3D structures of the complexes when available. In addition, we evaluate the impact of ligand labile protons on the WaterLOGSY data. Our results demonstrate that the WaterLOGSY experiment can be used as an additional confirmation of the binding mode of a ligand to a protein.

AB - WaterLOGSY is a sensitive ligand-observed NMR experiment for detection of interaction between a ligand and a protein and is now well-established as a screening technique for fragment-based lead discovery. Here we develop and assess a protocol to derive ligand epitope mapping from WaterLOGSY data and demonstrate its general applicability in studies of fragment-sized ligands binding to six different proteins (glycogen phosphorylase, protein peroxiredoxin 5, Bcl-xL, Mcl-1, HSP90, and human serum albumin). We compare the WaterLOGSY results to those obtained from the more widely used saturation transfer difference experiments and to the 3D structures of the complexes when available. In addition, we evaluate the impact of ligand labile protons on the WaterLOGSY data. Our results demonstrate that the WaterLOGSY experiment can be used as an additional confirmation of the binding mode of a ligand to a protein.

KW - binding mode

KW - fragment-based lead discovery

KW - saturation transfer difference

KW - solvent-exposed

KW - WaterLOGSY

UR - http://www.scopus.com/inward/record.url?scp=85068719629&partnerID=8YFLogxK

U2 - 10.1080/14756366.2019.1636235

DO - 10.1080/14756366.2019.1636235

M3 - Article

C2 - 31286785

AN - SCOPUS:85068719629

VL - 34

SP - 1218

EP - 1225

JO - JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY

JF - JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY

SN - 1475-6366

IS - 1

ER -