title: Protein-ligand binding affinity determination by the waterLOGSY method: An optimised approach considering ligand rebinding.
abstract: WaterLOGSY is a popular ligand-observed NMR technique to screen for protein-ligand interactions, yet when applied to measure dissociation constants (KD) through ligand titration, the results were found to be strongly dependent on sample conditions. Herein, we show that accurate KDs can be obtained by waterLOGSY with optimised experimental setup.
authors.affiliation: School of Chemical Sciences, The University of Auckland, Private Bag 92019, Victoria Street West, Auckland 1142, New Zealand.
authors.forename: Renjie
authors.initials: R
authors.lastname: Huang
authors.affiliation: Department of Chemistry, University of Oxford, Chemistry Research Laboratory, 12 Mansfield Road, Oxford OX1 3TA, United Kingdom.|Université D'Auvergne, 49 Boulevard François-Mitterrand, CS 60032, Clermont Ferrand 63001, Cedex 1, France.
authors.forename: Arnaud
authors.initials: A
authors.lastname: Bonnichon
authors.affiliation: Department of Chemistry, University of Oxford, Chemistry Research Laboratory, 12 Mansfield Road, Oxford OX1 3TA, United Kingdom.
authors.forename: Timothy D W
authors.initials: TD
authors.lastname: Claridge
authors.affiliation: School of Chemical Sciences, The University of Auckland, Private Bag 92019, Victoria Street West, Auckland 1142, New Zealand.
authors.forename: Ivanhoe K H
authors.initials: IK
authors.lastname: Leung
mesh_terms: D002110:Caffeine / Q000737:chemistry; D006801:Humans; D007700:Kinetics; D008024:Ligands; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D012709:Serum Albumin / Q000737:chemistry / Q000378:metabolism; D014364:Tryptophan / Q000737:chemistry
chemical_list: D008024:Ligands; D011506:Proteins; D012709:Serum Albumin; D002110:Caffeine; D014364:Tryptophan