Study of the mechanism of action of anoplin, a helical antimicrobial decapeptide with ion channel-like activity, and the role of the amidated C-terminus

Journal of Peptide Science

Volumn 14, Issue 6, 2008, Pages 661-669

  Cabrera, Marcia Perez Dos Santos ^a   Arcisio Miranda, Manoel ^a   Costa, Sabrina Thais Broggio ^b   Konno, Katsuhiro ^c   Ruggiero, José Roberto ^b   Procopio, Joaquim ^a   Neto, João Ruggiero ^b  

^a UNIVERSITY OF SÃO PAULO   (Brazil)

^b SÃO PAULO STATE UNIVERSITY UNESP   (Brazil)

^c INSTITUTO BUTANTAN   (Brazil)

Author keywords

Anoplin; Antimicrobial peptide; Ion channel; Lytic activity; Molecular dynamics; Peptide membrane interactions; Pore activity

Indexed keywords

ANOPLIN HYDROXIDE; ANOPLINAMIDE; ION CHANNEL; POLYPEPTIDE ANTIBIOTIC AGENT;

AMINO ACID SEQUENCE; ANTIMICROBIAL ACTIVITY; ARTICLE; BIOLOGICAL ACTIVITY; CARBOXY TERMINAL SEQUENCE; CHANNEL GATING; CIRCULAR DICHROISM; DEAMINATION; DRUG PURIFICATION; DRUG SYNTHESIS; ENZYME ACTIVITY; MINIMUM INHIBITORY CONCENTRATION; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN MODIFICATION; PROTEIN SECONDARY STRUCTURE;

AMIDES; ANTI-INFECTIVE AGENTS; ANTIMICROBIAL CATIONIC PEPTIDES; CIRCULAR DICHROISM; LIPID BILAYERS; WASP VENOMS;

BACTERIA (MICROORGANISMS);

EID: 47249140913     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.960     Document Type: Article

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