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Related Experiment Videos

Solution, solid phase and computational structures of apicidin and its backbone-reduced analogs.

Michael Kranz1, Peter John Murray, Stephen Taylor

  • 1GlaxoSmithKline Cambridge Chemistry Laboratory, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK. michael.j.kranz@gsk.com

Journal of Peptide Science : an Official Publication of the European Peptide Society
|December 13, 2005
PubMed
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Apicidin, a cyclic tetrapeptide (CTP), shows conformational flexibility in different solvents. Backbone reduction in CTP analogs preserves conformation and antiparasitic activity, aiding synthesis.

Area of Science:

  • Medicinal Chemistry
  • Structural Biology
  • Biochemistry

Background:

  • Apicidin is a rare, broad-spectrum antiparasitic cyclic tetrapeptide (CTP).
  • CTPs exhibit diverse backbone conformations influenced by solvent and amide bond rotation.
  • Understanding CTP conformation is crucial for drug design and synthesis.

Purpose of the Study:

  • To investigate the conformational behavior of apicidin and its analogs.
  • To explore the impact of backbone reduction on CTP conformation and activity.
  • To provide insights into the structure-activity relationship of apicidin.

Main Methods:

  • X-ray crystallography to determine solid-state structures.
  • Solution-state conformational analysis using NMR spectroscopy (implied by solvent dependence).

Related Experiment Videos

  • Computational conformational searches using the Amber force field.

    • Main Results:

    • Apicidin exhibits gamma-turns in dichloromethane and a beta-turn in DMSO.
    • X-ray structure reveals intermolecular hydrogen bonding stabilizing CTP stacks.
    • Backbone-reduced analogs mimic apicidin's DMSO conformation and retain antiparasitic activity.

    Conclusions:

    • CTP backbone conformation is adaptable and influenced by amide bond rotation.
    • Backbone reduction is a viable strategy to maintain CTP conformational preferences and biological activity.
    • This approach facilitates the synthesis of CTPs and related antiparasitic agents.