STD NMR and molecular modelling insights into interaction of novel mannose-based ligands with DC-SIGN

Org Biomol Chem. 2016 Jan 21;14(3):862-75. doi: 10.1039/c5ob01916h. Epub 2015 Nov 18.

Abstract

Study of interaction of mannose-based ligands with receptor DC-SIGN using high resolution NMR in combination with molecular modelling showed that four α-d-mannoside ligands interact with the binding site predominantly through the mannose moiety. The other two aromatic groups that are bound to α-d-mannose through a glycerol linker demonstrate interaction that can be related to their substitution pattern. Ligand with naphthyl and meta-substituted phenyl ring exhibited the most favourable binding characteristics. In addition to the predicted hydrophobic interactions of aromatic moieties our results propose new contacts of substituted phenyl moiety in the more polar area of the flat binding site of DC-SIGN and thus offer new possibilities in further designing of novel, more potent DC-SIGN antagonists.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Cell Adhesion Molecules / antagonists & inhibitors
  • Cell Adhesion Molecules / chemistry*
  • Cell Adhesion Molecules / metabolism*
  • Humans
  • Lectins, C-Type / antagonists & inhibitors
  • Lectins, C-Type / chemistry*
  • Lectins, C-Type / metabolism*
  • Ligands
  • Magnetic Resonance Spectroscopy
  • Mannose / chemistry*
  • Mannose / metabolism*
  • Mannose / pharmacology
  • Models, Molecular*
  • Molecular Structure
  • Receptors, Cell Surface / antagonists & inhibitors
  • Receptors, Cell Surface / chemistry*
  • Receptors, Cell Surface / metabolism*
  • Structure-Activity Relationship

Substances

  • Cell Adhesion Molecules
  • DC-specific ICAM-3 grabbing nonintegrin
  • Lectins, C-Type
  • Ligands
  • Receptors, Cell Surface
  • Mannose