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Biochimica et Biophysica Acta - Biomembranes

Volumn 1462, Issue 1-2, 1999, Pages 71-87

Structural features of helical antimicrobial peptides: Their potential to modulate activity on model membranes and biological cells

(2) Dathe, Margitta a Wieprecht, Torsten b

a LEIBNIZ INSTITUT FÜR MOLEKULARE PHARMAKOLOGIE (Germany)

b UNIVERSITY OF BASEL (Switzerland)

Author keywords

Amphipathicity; Antimicrobial peptides; Helicity; Hydrophobic moment; Hydrophobicity; Membrane activity; Peptide charge; Polar hydrophobic angle

Indexed keywords

CECROPIN; MAGAININ DERIVATIVE; MELITTIN; PEPTIDE DERIVATIVE;

ANTIMICROBIAL ACTIVITY; BILAYER MEMBRANE; DRUG CONFORMATION; DRUG SELECTIVITY; DRUG STRUCTURE; HYDROPHOBICITY; MEMBRANE STABILIZATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN INTERACTION; PROTEIN STRUCTURE; REVIEW; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; ANIMALS; ANTI-BACTERIAL AGENTS; ANTIMICROBIAL CATIONIC PEPTIDES; BACTERIA; CELL MEMBRANE; ELECTROSTATICS; ERYTHROCYTE MEMBRANE; LIPID BILAYERS; MELITTEN; MEMBRANE LIPIDS; MOLECULAR SEQUENCE DATA; PEPTIDES; PERMEABILITY; PROTEIN STRUCTURE, SECONDARY; STRUCTURE-ACTIVITY RELATIONSHIP; XENOPUS PROTEINS;

ANIMALIA; PROKARYOTA;

EID: 0032719739 PISSN: 00052736 EISSN: None Source Type: Journal
DOI: 10.1016/S0005-2736(99)00201-1 Document Type: Review

Times cited : (675)

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