Effect of disulphide bond position on salt resistance and LPS-neutralizing activity of α-helical homo-dimeric model antimicrobial peptides

BMB Reports

Volumn 44, Issue 11, 2011, Pages 747-752

  Nan, Yong Hai ^a   Shin, Song Yub ^a,b  

^a Chosun University   (South Korea)

^b Chosun University College of Medicine   (South Korea)

Author keywords

Antimicrobial peptide; Disulphide bond; Homo dimeric helical peptide; LPS neutralizing activity; Salt resistance

Indexed keywords

ANTIMICROBIAL CATIONIC PEPTIDE; COLORING AGENT; DISULFIDE; LIPOPOLYSACCHARIDE; NITRIC OXIDE; SODIUM CHLORIDE;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; BACTERIUM; BIOSYNTHESIS; CELL LINE; CHEMISTRY; DRUG EFFECT; HEMOLYSIS; HUMAN; KINETICS; METABOLISM; MICROBIOLOGICAL EXAMINATION; MOLECULAR GENETICS; MOUSE; PROTEIN MULTIMERIZATION; PROTEIN SECONDARY STRUCTURE; SERODIAGNOSIS; SYNTHESIS;

AMINO ACID SEQUENCE; ANIMALS; ANTIMICROBIAL CATIONIC PEPTIDES; BACTERIA; CELL LINE; COLORING AGENTS; DISULFIDES; HEMOLYSIS; HUMANS; KINETICS; LIPOPOLYSACCHARIDES; MICE; MICROBIAL SENSITIVITY TESTS; MOLECULAR SEQUENCE DATA; NEUTRALIZATION TESTS; NITRIC OXIDE; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; SODIUM CHLORIDE;

EID: 84857768642     PISSN: 19766696     EISSN: 1976670X     Source Type: Journal    
DOI: 10.5483/BMBRep.2011.44.11.747     Document Type: Article

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