Structure and functions of channel-forming peptides: magainins, cecropins, melittin and alamethicin

J Membr Biol. 1997 Apr 1;156(3):197-211. doi: 10.1007/s002329900201.
No abstract available

Publication types

  • Comparative Study
  • Review

MeSH terms

  • Alamethicin / chemistry*
  • Alamethicin / pharmacology
  • Amino Acid Sequence
  • Animals
  • Anti-Bacterial Agents / chemistry
  • Anti-Bacterial Agents / pharmacology
  • Antimicrobial Cationic Peptides*
  • Cell Membrane Permeability / drug effects
  • Energy Metabolism
  • Insect Proteins / chemistry*
  • Insect Proteins / pharmacology
  • Insect Proteins / physiology
  • Ion Channels / chemistry*
  • Lipid Bilayers
  • Magainins
  • Melitten / chemistry*
  • Melitten / pharmacology
  • Melitten / physiology
  • Membrane Potentials / drug effects
  • Molecular Sequence Data
  • Peptides / chemistry*
  • Peptides / pharmacology
  • Peptides / physiology
  • Sheep
  • Structure-Activity Relationship
  • Xenopus Proteins*

Substances

  • Anti-Bacterial Agents
  • Antimicrobial Cationic Peptides
  • Insect Proteins
  • Ion Channels
  • Lipid Bilayers
  • Magainins
  • Peptides
  • Xenopus Proteins
  • magainin 2 peptide, Xenopus
  • Melitten
  • Alamethicin
  • cecropin A