New biophysical probes for structure-activity analyses of vacuolar-H+ -ATPase enzymes

Org Biomol Chem. 2003 Dec 21;1(24):4361-3. doi: 10.1039/b311401e. Epub 2003 Nov 3.

Abstract

New EPR spin labelled and photoactivatable molecules have been designed to probe specifically the vacuolar-H(+)-ATPase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alkenes / chemical synthesis
  • Alkenes / pharmacology*
  • Amides / chemical synthesis
  • Amides / pharmacology
  • Electron Spin Resonance Spectroscopy
  • Enzyme Inhibitors / chemical synthesis*
  • Enzyme Inhibitors / pharmacology
  • Indoles / chemical synthesis
  • Indoles / pharmacology*
  • Isomerism
  • Models, Biological
  • Models, Chemical
  • Molecular Structure
  • Piperidines / chemical synthesis
  • Piperidines / pharmacology*
  • Spin Labels
  • Structure-Activity Relationship
  • Temperature
  • Vacuolar Proton-Translocating ATPases / antagonists & inhibitors
  • Vacuolar Proton-Translocating ATPases / chemistry*
  • Vacuolar Proton-Translocating ATPases / metabolism
  • Yeasts / drug effects
  • Yeasts / enzymology

Substances

  • (2Z,4E)-5-(5,6-dichloro-2-indolyl)-2-methoxy-N-(4-(2,2,6,6- tetramethylpiperidinoxy))-2,4-pentadienamide
  • Alkenes
  • Amides
  • Enzyme Inhibitors
  • Indoles
  • Piperidines
  • Spin Labels
  • Vacuolar Proton-Translocating ATPases