Ideally amphipathic β-sheeted peptides at interfaces: Structure, orientation, affinities for lipids and hemolytic activity of (KL)(m)K peptides

Biochimica et Biophysica Acta - Biomembranes

Volumn 1463, Issue 1, 2000, Pages 65-80

  Castano, Sabine ^a   Desbat, Bernard ^b   Dufourcq, Jean ^a  

^a CNRS   (France)

^b UNIVERSITÉ DE BORDEAUX   (France)

Author keywords

Sheeted peptide; Cytotoxic; Fluorescence; FT IR spectroscopy; Lipid peptide interaction; Monolayer; Phospholipid vesicle; Polarization modulated IRRAS

Indexed keywords

DIMYRISTOYLPHOSPHATIDYLCHOLINE; PEPTIDE; PHOSPHOLIPID;

ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; CYTOTOXICITY; FLUORESCENCE; FLUORESCENCE SPECTROSCOPY; HEMOLYSIS; HUMAN; HUMAN CELL; INFRARED SPECTROSCOPY; PHOSPHOLIPID VESICLE; POLARIZATION; PRIORITY JOURNAL; PROTEIN LIPID INTERACTION; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; DIMYRISTOYLPHOSPHATIDYLCHOLINE; DRUG DESIGN; HEMOLYSIS; HUMANS; LIPID METABOLISM; LIPOSOMES; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN STRUCTURE, SECONDARY; SOLUTIONS; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; STRUCTURE-ACTIVITY RELATIONSHIP; WATER;

EID: 0033957859     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2736(99)00175-3     Document Type: Article

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