Structure-function studies on the amphibian peptide brevinin 1E: Translocating the cationic segment from the C-terminal end to a central position favors selective antibacterial activity

Journal of Peptide Research

Volumn 58, Issue 5, 2001, Pages 433-441

  Kumari, V K ^a   Nagaraj, R ^a  

^a CENTRE FOR CELLULAR AND MOLECULAR BIOLOGY   (India)

Author keywords

Amphibian skin secretions; Antimicrobial peptides; Hemolytic activity; Lipid interactions; Secondary structure

Indexed keywords

BREVININ 1E; PEPTIDE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANIMAL TISSUE; ANTIBACTERIAL ACTIVITY; ARTICLE; CARBOXY TERMINAL SEQUENCE; HEMOLYSIS; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN LIPID INTERACTION; PROTEIN SECONDARY STRUCTURE; SEQUENCE ANALYSIS; STRUCTURE ACTIVITY RELATION;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; AMPHIBIAN PROTEINS; ANIMALS; ANTI-BACTERIAL AGENTS; ANTI-INFECTIVE AGENTS; ANTIMICROBIAL CATIONIC PEPTIDES; CATIONS; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CIRCULAR DICHROISM; DISULFIDES; FLUORESCEINS; LIPIDS; MOLECULAR SEQUENCE DATA; PEPTIDE BIOSYNTHESIS; PROTEIN STRUCTURE, TERTIARY; RANA ESCULENTA; STRUCTURE-ACTIVITY RELATIONSHIP; TIME FACTORS;

AMPHIBIA; ANIMALIA; ANURA; RANA ESCULENTA; RANA TEMPORARIA;

EID: 0035187785     PISSN: 1397002X     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1399-3011.2001.00924.x     Document Type: Article

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