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

Journal of Membrane Biology

Volumn 156, Issue 3, 1997, Pages 197-211

  Bechinger, B ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

Helical bundle; Bilayer disruption; Hemolysis; Peptide antibiotics; Pore formation; Protein lipid interactions

Indexed keywords

ALAMETHICIN; CECROPIN; ION CHANNEL; MAGAININ DERIVATIVE; MELITTIN; MEMBRANE PROTEIN; PEPTIDE; POLYPEPTIDE ANTIBIOTIC AGENT;

CHANNEL GATING; CHEMICAL STRUCTURE; CONDUCTANCE; DRUG ACTIVITY; HUMAN; LIPID BILAYER; NONHUMAN; REVIEW;

ALAMETHICIN; AMINO ACID SEQUENCE; ANIMALS; ANTI-BACTERIAL AGENTS; ANTIMICROBIAL CATIONIC PEPTIDES; CELL MEMBRANE PERMEABILITY; ENERGY METABOLISM; INSECT PROTEINS; ION CHANNELS; LIPID BILAYERS; MELITTEN; MEMBRANE POTENTIALS; MOLECULAR SEQUENCE DATA; PEPTIDES; SHEEP; STRUCTURE-ACTIVITY RELATIONSHIP; XENOPUS PROTEINS;

EID: 0030981655     PISSN: 00222631     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002329900201     Document Type: Review

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