Conformational Changes in Small Ligands Upon Tetanus Toxin Binding

Abstract

To understand the processes associated with small synthetic ligands binding large protein surfaces, NMR spectroscopy was used to examine the conformational changes in doxorubicin and lavendustin A upon binding to tetanus toxin. C13 T1 measurements suggested that to a first approximation, the conformational behavior of doxorubicin in solution appears to be a composite of a rigid aromatic ring system, ring librations for its cyclohexane and carbohydrate rings, and segmental motions for the pendant C(O)CH2OH group. trNOESY experiments indicated that both ligands adopt rigid conformations when bound to tetanus toxin and each binds a different site on the toxin surface.

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Document Details

Document Type
Technical Report
Publication Date
Jun 01, 2008
Accession Number
ADA485965

Entities

People

  • Rossitza K. Gitti
  • Terry J. Henderson

Organizations

  • Edgewood Chemical Biological Center

Tags

Communities of Interest

  • Energy and Power Technologies

DTIC Thesaurus Topics

  • Acquisition
  • Carbohydrates
  • Chemical Shifts
  • Chemistry
  • Composite Materials
  • Computers
  • Data Sets
  • Detection
  • Fourier Transformation
  • Macromolecules
  • Magnetic Resonance
  • Materials
  • Measurement
  • Molecules
  • Nuclear Magnetic Resonance
  • Small Molecules
  • Spectroscopy

Fields of Study

  • Chemistry

Readers

  • Molecular and Cellular Biochemistry
  • Polymer Science and Technology
  • Quantum spin resonance or Electron Paramagnetic Resonance spectroscopy.