Designed low amphipathic peptides with α-helical propensity exhibiting antimicrobial activity via a lipid domain formation mechanism

Peptides

Volumn 31, Issue 5, 2010, Pages 794-805

  Yamamoto, Naoki ^a   Tamura, Atsuo ^a  

^a KOBE UNIVERSITY   (Japan)

Author keywords

Antimicrobial peptide; Domain formation mechanism; Low amphipathicity

Indexed keywords

ANION; CALCEIN; LIPID; LIPOSOME; PEPTIDE DERIVATIVE; PROTEIN LAP1; PROTEIN LAP2; PROTEIN LAP3; PROTEIN LAP4; PROTEIN LAP6; UNCLASSIFIED DRUG;

ALPHA HELIX; ANTIMICROBIAL ACTIVITY; ARTICLE; BACILLUS SUBTILIS; CONTROLLED STUDY; DRUG DESIGN; DRUG SYNTHESIS; ESCHERICHIA COLI; HYDROPHOBICITY; LIPID MEMBRANE; MEMBRANE BINDING; MEMBRANE DAMAGE; MEMBRANE FLUIDITY; MEMBRANE TRANSPORT; MINIMUM INHIBITORY CONCENTRATION; NONHUMAN; PRIORITY JOURNAL;

ANIMALS; ANTI-INFECTIVE AGENTS; BACILLUS CEREUS; CALORIMETRY, DIFFERENTIAL SCANNING; CELLS, CULTURED; CIRCULAR DICHROISM; ESCHERICHIA COLI; HEMOLYSIS; LIPOSOMES; MAGNETIC RESONANCE SPECTROSCOPY; MICROBIAL SENSITIVITY TESTS; PEPTIDES; PROTEIN STRUCTURE, SECONDARY; SHEEP;

BACILLUS SUBTILIS; ESCHERICHIA COLI;

EID: 77951253196     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2010.01.006     Document Type: Article

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