A binding mode hypothesis of tiagabine confirms liothyronine effect on γ-aminobutyric acid transporter 1 (GAT1)

J Med Chem. 2015 Mar 12;58(5):2149-58. doi: 10.1021/jm5015428. Epub 2015 Feb 26.

Abstract

Elevating GABA levels in the synaptic cleft by inhibiting its reuptake carrier GAT1 is an established approach for the treatment of CNS disorders like epilepsy. With the increasing availability of crystal structures of transmembrane transporters, structure-based approaches to elucidate the molecular basis of ligand-transporter interaction also become feasible. Experimental data guided docking of derivatives of the GAT1 inhibitor tiagabine into a protein homology model of GAT1 allowed derivation of a common binding mode for this class of inhibitors that is able to account for the distinct structure-activity relationship pattern of the data set. Translating essential binding features into a pharmacophore model followed by in silico screening of the DrugBank identified liothyronine as a drug potentially exerting a similar effect on GAT1. Experimental testing further confirmed the GAT1 inhibiting properties of this thyroid hormone.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Computer Simulation
  • GABA Agonists / chemistry
  • GABA Agonists / metabolism*
  • GABA Plasma Membrane Transport Proteins / chemistry*
  • GABA Plasma Membrane Transport Proteins / metabolism*
  • HEK293 Cells
  • High-Throughput Screening Assays
  • Humans
  • Models, Molecular
  • Molecular Docking Simulation*
  • Molecular Structure
  • Nipecotic Acids / chemistry
  • Nipecotic Acids / metabolism*
  • Structure-Activity Relationship
  • Tiagabine
  • Triiodothyronine / chemistry
  • Triiodothyronine / pharmacology*
  • gamma-Aminobutyric Acid / metabolism*

Substances

  • GABA Agonists
  • GABA Plasma Membrane Transport Proteins
  • Nipecotic Acids
  • SLC6A1 protein, human
  • Triiodothyronine
  • gamma-Aminobutyric Acid
  • Tiagabine