Dimerization of aurein 1.2: Effects in structure, antimicrobial activity and aggregation of Cândida albicans cells

Amino Acids

Volumn 44, Issue 6, 2013, Pages 1521-1528

  Lorenzon E N ^a   Sanches, P R S ^a   Nogueira, L G ^a   Bauab, T M ^a   Cilli, E M ^a  

^a SÃO PAULO STATE UNIVERSITY UNESP   (Brazil)

Author keywords

Antimicrobial peptides; Aurein 1.2; Biological activity; Dimerization; Secondary structure

Indexed keywords

AUREIN 1.2; LYSOPHOSPHATIDYLCHOLINE; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ANTIBACTERIAL ACTIVITY; ANTIFUNGAL ACTIVITY; ANTIMICROBIAL ACTIVITY; ARTICLE; CANDIDA ALBICANS; CARBOXY TERMINAL SEQUENCE; CELL AGGREGATION; CELL PERMEABILIZATION; CELL VACUOLE; CIRCULAR DICHROISM; CONCENTRATION RESPONSE; CONTROLLED STUDY; DIMERIZATION; FUNGAL CELL; HEMOLYSIS; HUMAN; HUMAN CELL; MICELLE; MICROBIAL ADHESION; MINIMUM INHIBITORY CONCENTRATION; NONHUMAN; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN STRUCTURE; SOLID PHASE SYNTHESIS;

ANTI-INFECTIVE AGENTS; ANTIMICROBIAL CATIONIC PEPTIDES; CANDIDA ALBICANS; CIRCULAR DICHROISM; ESCHERICHIA COLI; HEMOLYSIS; HUMANS; MICROBIAL SENSITIVITY TESTS; PERMEABILITY; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; SOLID-PHASE SYNTHESIS TECHNIQUES; STAPHYLOCOCCUS AUREUS; STRUCTURE-ACTIVITY RELATIONSHIP;

CANDIDA ALBICANS; FUNGI;

EID: 84878221033     PISSN: 09394451     EISSN: 14382199     Source Type: Journal    
DOI: 10.1007/s00726-013-1475-3     Document Type: Article

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