Addition of a small hydrophobic segment from the head region to an amphipathic leucine zipper like motif of E. coli toxin hemolysin E enhances the peptide-induced permeability of zwitterionic lipid vesicles

Biochimica et Biophysica Acta - Biomembranes

Volumn 1768, Issue 6, 2007, Pages 1574-1582

  Yadav, Sharada Prasad ^a   Ahmad, Aqeel ^a   Ghosh, Jimut Kanti ^a  

^a CENTRAL DRUG RESEARCH INSTITUTE   (India)

Author keywords

Fluorescence and flow cytometric studies; Membrane permeability; Membrane assembly of hemolysin E derived peptides; Membrane interaction of hemolysin E; Peptide lipid interaction; Zwitterionic and negatively charged lipid vesicles

Indexed keywords

AMPHOLYTE; ESCHERICHIA COLI ENDOTOXIN; FLUORESCENT DYE; H 198 PEPTIDE; H 205 PEPTIDE; HEMOLYSIN; HEMOLYSIN E; LEUCINE ZIPPER PROTEIN; MUTANT PROTEIN; PEPTIDE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CELL MEMBRANE PERMEABILITY; ENERGY TRANSFER; FLOW CYTOMETRY; HYDROPHOBICITY; LIPID VESICLE; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN STRUCTURE; PROTEIN SYNTHESIS;

AMINO ACID SEQUENCE; CIRCULAR DICHROISM; ESCHERICHIA COLI PROTEINS; FLOW CYTOMETRY; HEMOLYSIN PROTEINS; LEUCINE ZIPPERS; MOLECULAR SEQUENCE DATA; PERMEABILITY; PROTEIN CONFORMATION; PROTEIN ENGINEERING; TRANSPORT VESICLES;

EID: 34249042323     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2007.03.019     Document Type: Article

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