A hemocyanin-derived antimicrobial peptide from the penaeid shrimp adopts an alpha-helical structure that specifically permeabilizes fungal membranes

Biochimica et Biophysica Acta - General Subjects

Volumn 1860, Issue 3, 2016, Pages 557-568

  Petit, Vanessa W ^a,e   Rolland, Jean Luc ^b   Blond, Alain ^a   Cazevieille, Chantal ^d   Djediat, Chakib ^a   Peduzzi, Jean ^a   Goulard, Christophe ^a   Bachère, Evelyne ^b   Dupont, Joëlle ^c   Destoumieux Garzón, Delphine ^b   Rebuffat, Sylvie ^a  

^a SORBONNE UNIVERSITÉ   (France)

^b UNIV MONTPELLIER   (France)

^c Cedex   (France)

^d University of Montpellier   (France)

^e INSTITUT DE RADIOPROTECTION ET DE SÛRETÉ NUCLÉAIRE   (France)

Author keywords

Amphipathic helix; Antimicrobial peptide; Fluorescence microscopy; Fungi; Membrane bilayer; Nuclear magnetic resonance (NMR)

Indexed keywords

CARBOXY TERMINAL HEMOCYANIN; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG; ANTIMICROBIAL CATIONIC PEPTIDE; HEMOCYANIN;

ALPHA HELIX; ANTIFUNGAL ACTIVITY; ARTICLE; CYTOLYSIS; CYTOPLASM; DRUG CONFORMATION; DRUG STRUCTURE; FUNGAL CELL WALL; FUNGAL MEMBRANE; FUNGUS HYPHAE; FUNGUS SPORE; FUSARIUM OXYSPORUM; LITOPENAEUS VANNAMEI; MEMBRANE PERMEABILITY; MINIMUM INHIBITORY CONCENTRATION; NONHUMAN; PRIORITY JOURNAL; ANIMAL; CELL MEMBRANE; CHEMISTRY; DRUG EFFECTS; FUSARIUM; METABOLISM; PENAEIDAE; PERMEABILITY; PH; PROTEIN SECONDARY STRUCTURE; ULTRASTRUCTURE;

ANIMALS; ANTIMICROBIAL CATIONIC PEPTIDES; CELL MEMBRANE; FUSARIUM; HEMOCYANIN; HYDROGEN-ION CONCENTRATION; HYPHAE; PENAEIDAE; PERMEABILITY; PROTEIN STRUCTURE, SECONDARY; SPORES, FUNGAL;

EID: 84954341898     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2015.12.010     Document Type: Article

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