Evaluation of Solvent Accessibility Epitopes for Different Dehydrogenase Inhibitors

Christian Ludwig, P Michiels, Alessia Lodi, Jonathan Ride, Christopher Bunce, Ulrich Gunther

Research output: Contribution to journalArticle

15 Citations (Scopus)


Knowledge about the orientation of ligands or inhibitors bound to a protein is vital for the development of new drugs. It was recently shown that solvent accessibility epitopes for protein ligands can be mapped by transferring magnetization from water molecules to the ligand to derive the ligand orientation. This is based on the fact that NMR signals of ligands arising from magnetization transferred from solvent molecules via the protein have a different sign from those arising from direct magnetization transfer from bulk water. Herein we critically evaluate the applicability of solvent accessibility mapping to derive binding orientations for ligands of two dehydrogenases (AKR1C3 and HSD17beta1) with very different binding pockets, including complexes in which the ligand is buried more deeply inside the protein. We also evaluate the possibility of using co-solvents, such as DMSO, for magnetization transfer.
Original languageEnglish
Pages (from-to)1371-1376
Number of pages6
Issue number9
Publication statusPublished - 15 Sept 2008


  • NMR spectroscopy
  • protein-ligand interactions
  • pharmacophore mapping
  • epitope mapping


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