Consequences of isostructural main-chain modifications for the design of antimicrobial foldamers: helical mimics of host-defense peptides based on a heterogeneous amide/urea backbone

Angew Chem Int Ed Engl. 2010;49(2):333-6. doi: 10.1002/anie.200905591.
No abstract available

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amides / chemical synthesis
  • Amides / chemistry
  • Anti-Infective Agents / chemistry*
  • Anti-Infective Agents / pharmacology*
  • Candida / drug effects
  • Cell Membrane / chemistry
  • Cell Membrane / drug effects
  • Drug Design
  • Escherichia coli / drug effects
  • Microbial Sensitivity Tests
  • Microscopy, Immunoelectron
  • Molecular Conformation
  • Molecular Mimicry
  • Peptides / chemistry*
  • Peptides / pharmacology*
  • Protein Folding
  • Protein Structure, Secondary
  • Pseudomonas aeruginosa / drug effects
  • Staphylococcus aureus / drug effects
  • Structure-Activity Relationship
  • Urea / chemical synthesis
  • Urea / chemistry

Substances

  • Amides
  • Anti-Infective Agents
  • Peptides
  • Urea