Chimerization of lactoferricin and lactoferrampin peptides strongly potentiates the killing activity against Candida albicans

Biochemistry and Cell Biology

Volumn 90, Issue 3, 2012, Pages 378-388

  Bolscher, Jan ^a   Nazmi, Kamran ^a   Van Marle, Jan ^b   Van 'T Hof, Wim ^a   Veerman, Enno ^a  

^a UNIVERSITY OF AMSTERDAM   (Netherlands)

^b UNIVERSITY OF AMSTERDAM   (Netherlands)

Author keywords

Candida albicans; Lactoferrampin; Lactoferricin; LFchimera; Pseudohyphae; Yeast

Indexed keywords

CANDIDA ALBICANS; LACTOFERRAMPIN; LACTOFERRICIN; LFCHIMERA; PSEUDOHYPHAE;

ACTIVATION ANALYSIS; AMINO ACIDS; BACTERICIDES; CANDIDA; ELECTRON MICROSCOPY; IONIC STRENGTH; MAMMALS; YEAST;

PEPTIDES;

ADENOSINE TRIPHOSPHATE; ASPARTYLLEUCYLISOLEUCYLTRYPTOPHYLLYSYLLEUCYLLEUCYLSERYLLYSYLALANYLGLUTAMINYLGLUTAMYLLYSYLPHENYLALANYLGLYCYLLYSYLASPARAGINYLLYSYLSERYLARGININE; CHIMERIC LACTOFERRIN; CHIMERIC PROTEIN; LACTOFERRAMPIN; LACTOFERRICIN; LACTOFERRIN; PEPTIDE FRAGMENT; PHENYLALANYLLYSYLCYSTEINYLARGINYLARGINYLTRYPTOPHYLGLUTAMINYLTRYPTOPHYLARGINYLMETHIONYLLYSYLLYSYLLEUCYLGLYCINE; POLYPEPTIDE ANTIBIOTIC AGENT; PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BILAYER MEMBRANE; CANDIDA ALBICANS; CELL MEMBRANE; CELL MEMBRANE PERMEABILITY; CELL ULTRASTRUCTURE; CHIMERIZATION; CONCENTRATION RESPONSE; CONTROLLED STUDY; DRUG DESIGN; DRUG EFFECT; DRUG MECHANISM; DRUG POTENTIATION; ELECTRON MICROSCOPY; FLUORESCENCE MICROSCOPY; FREEZE FRACTURE ELECTRON MICROSCOPY; FUNGICIDAL ACTIVITY; MEMBRANE DAMAGE; MEMBRANE STRUCTURE; MEMBRANE TRANSPORT; MOLECULAR WEIGHT; NONHUMAN; PEPTIDE SYNTHESIS; PROTEIN MODIFICATION; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; TANDEM MASS SPECTROMETRY;

AMINO ACID SEQUENCE; ANIMALS; ANTIFUNGAL AGENTS; CANDIDA ALBICANS; CATTLE; CELL MEMBRANE; FLUORESCENT DYES; FUNGAL PROTEINS; LACTOFERRIN; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PERMEABILITY; PROPIDIUM; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT FUSION PROTEINS;

BOVINAE; CANDIDA ALBICANS;

EID: 84861371938     PISSN: 08298211     EISSN: 12086002     Source Type: Journal    
DOI: 10.1139/o11-085     Document Type: Article

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