Characterization of the antimicrobial peptide derived from sapecin B, an antibacterial protein of Sarcophaga peregrina (flesh fly).
Sapecin B, an antibacterial protein of Sarcophaga peregrina, was divided into four peptides. A hendecapeptide derived from its helix region was found to have comparable antibacterial activity with that of the complete protein. This peptide had a much wider spectrum of antimicrobial activity than that of sapecin B, exhibiting activity on not only Staphylococcus aureus (Gram-positive) and Escherichia coli (Gram-negative), but also some yeasts, including Candida albicans. The peptide was shown to bind to liposomes containing acidic phospholipids and cause release of entrapped glucose, suggesting that its primary site of action is the bacterial membrane. Its antimicrobial activity could be increased by substituting various amino acid residues for hydrophobic and/or basic ones.
Yamada
K
K
Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
Natori
S
S
D000595:Amino Acid Sequence; D000818:Animals; D001419:Bacteria / Q000187:drug effects*; D001894:Borohydrides / Q000494:pharmacology; D002176:Candida albicans / Q000187:drug effects; D004175:Diptera / Q000737:chemistry*; D004228:Dithionitrobenzoic Acid / Q000494:pharmacology; D004926:Escherichia coli / Q000187:drug effects; D007301:Insect Hormones / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology*; D019476:Insect Proteins; D008081:Liposomes / Q000378:metabolism; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology*; D010743:Phospholipids / Q000378:metabolism; D013211:Staphylococcus aureus / Q000187:drug effects; D013329:Structure-Activity Relationship
D001894:Borohydrides; D007301:Insect Hormones; D019476:Insect Proteins; D008081:Liposomes; D010446:Peptide Fragments; D010743:Phospholipids; C080667:sapecin B protein, Sarcophaga peregrina; C025364:sodium borohydride; D004228:Dithionitrobenzoic Acid