Controlled alteration of the shape and conformational stability of α-helical cell-lytic peptides: Effect on mode of action and cell specificity

Biochemical Journal

Volumn 390, Issue 1, 2005, Pages 177-188

  Zelezetsky, Igor ^a   Pacor, Sabrina ^a   Pag, Ulrike ^b   Papo, Niv ^c   Shai, Yechiel ^c   Sahl, Hans Georg ^b   Tossi, Alessandro ^a  

^a UNIVERSITY OF TRIESTE   (Italy)

^b UNIVERSITY OF BONN   (Germany)

^c WEIZMANN INSTITUTE OF SCIENCE   (Israel)

Author keywords

Amphipathic helix; Antimicrobial peptide; Cell specificity; Cell lytic peptide; Mode of action; Surface plasmon resonance

Indexed keywords

CELLS; HYDROPHOBICITY; POLYPEPTIDES; SURFACE PLASMON RESONANCE;

CELL SPECIFITY; CELL-LYTIC-PEPTIDE; MODE OF ACTION;

CONFORMATIONS;

CARBON; CHOLESTEROL; PHOSPHATIDYLCHOLINE; SYNTHETIC PEPTIDE;

ALPHA HELIX; ANTIMICROBIAL ACTIVITY; ARTICLE; CELL SPECIFICITY; CONFORMATIONAL TRANSITION; CYTOFLUOROMETRY; CYTOTOXICITY; ESCHERICHIA COLI; EUKARYOTIC CELL; HEMOLYSIS; HOST CELL; HYDROPHOBICITY; LYMPHOCYTE; PRIORITY JOURNAL; PROTEIN STRUCTURE; STAPHYLOCOCCUS AUREUS; SURFACE PLASMON RESONANCE;

AMINO ACID SEQUENCE; ANTI-BACTERIAL AGENTS; ANTIFUNGAL AGENTS; BACTERIA; CELL MEMBRANE; FUNGI; PEPTIDES; PERMEABILITY; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY;

EUKARYOTA;

EID: 23944500330     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20042138     Document Type: Article

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