Real-time monitoring of conformational transitions of single-molecule histone deacetylase 8 with nanocircuits

Chem Commun (Camb). 2017 Mar 16;53(23):3307-3310. doi: 10.1039/c6cc09949a.

Abstract

Using single-molecule approaches, we directly observed the dynamic interaction between HDAC8 and various ligands as well as conformational interconversions during the catalytic reaction. Statistical analysis identified key kinetic parameters, demonstrating that the enzymatic activity is highly sensitive to both minor variations in the ligand structures and small synthetic molecules.

MeSH terms

  • Electric Conductivity
  • Equipment Design
  • Histone Deacetylase Inhibitors / chemistry
  • Histone Deacetylases / chemistry*
  • Humans
  • Hydroxamic Acids / chemistry
  • Kinetics
  • Ligands
  • Nanotechnology / instrumentation*
  • Nanotubes, Carbon / chemistry*
  • Protein Conformation
  • Repressor Proteins / chemistry*
  • Vorinostat

Substances

  • Histone Deacetylase Inhibitors
  • Hydroxamic Acids
  • Ligands
  • Nanotubes, Carbon
  • Repressor Proteins
  • Vorinostat
  • HDAC8 protein, human
  • Histone Deacetylases